CAZypedia - User contributions [en-ca]

Carbohydrate Binding Module Family 70

2024-11-13T03:21:11Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin <cite>Michael2014</cite>. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family. This groove, which is similar to the binding site observed in β-sandwich CBMs such as those in the CBM4 family, is the putative hyaluronan-binding site <cite>Alisdair2002</cite>. Structural studies and mutational analysis have identified key residues, including a conserved solvent-exposed tryptophan and several basic residues, that are essential for hyaluronan recognition, supporting its classification as a Type B CBM <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, the CBM70 family member SrCBM70 has been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating its potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Alisdair2002 pmid=12079353

#Daniel2003 pmid=12833544

#Brandi2009 pmid=18838391

#Alisdair2004 pmid=15214846

#Luciane2002 pmid=12130645

#Kostyukova1995 pmid=7719281

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-11-10T09:11:16Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin <cite>Michael2014</cite>. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family. This groove, which is similar to the binding site observed in β-sandwich CBMs such as those in the CBM4 family, is the putative hyaluronan-binding site <cite>Alisdair2002</cite>. Structural studies and mutational analysis have identified key residues, including a conserved solvent-exposed tryptophan and several basic residues, that are essential for hyaluronan recognition, supporting its classification as a Type B CBM <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Alisdair2002 pmid=12079353

#Daniel2003 pmid=12833544

#Brandi2009 pmid=18838391

#Alisdair2004 pmid=15214846

#Luciane2002 pmid=12130645

#Kostyukova1995 pmid=7719281

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-11-10T09:10:42Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin <cite>Michael2014</cite>. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family. This groove, which is similar to the binding site observed in β-sandwich CBMs such as those in the CBM4 family, is the putative hyaluronan-binding site <cite>Alisdair2002</cite>. Structural studies and mutational analysis have identified key residues, including a conserved solvent-exposed tryptophan and several basic residues, that are essential for hyaluronan recognition, supporting its classification as a Type B CBM <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Alisdair2002 pmid:12079353

#Daniel2003 pmid=12833544

#Brandi2009 pmid=18838391

#Alisdair2004 pmid=15214846

#Luciane2002 pmid=12130645

#Kostyukova1995 pmid=7719281

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-11-10T09:08:30Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin <cite>Michael2014</cite>. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family. This groove, which is similar to the binding site observed in β-sandwich CBMs such as those in the CBM4 family, is the putative hyaluronan-binding site. Structural studies and mutational analysis have identified key residues, including a conserved solvent-exposed tryptophan and several basic residues, that are essential for hyaluronan recognition, supporting its classification as a Type B CBM <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Daniel2003 pmid=12833544

#Brandi2009 pmid=18838391

#Alisdair2004 pmid=15214846

#Luciane2002 pmid=12130645

#Kostyukova1995 pmid=7719281

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-11-08T14:15:35Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin <cite>Michael2014</cite>. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Daniel2003 pmid=12833544

#Brandi2009 pmid=18838391

#Alisdair2004 pmid=15214846

#Luciane2002 pmid=12130645

#Kostyukova1995 pmid=7719281

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-11-08T14:13:41Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Michael2014 Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Daniel2003 pmid=12833544

#Brandi2009 pmid=18838391

#Alisdair2004 pmid=15214846

#Luciane2002 pmid=12130645

#Kostyukova1995 pmid=7719281

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-11-08T14:11:46Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Michael2014 Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets <cite>Michael2014</cite>.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid <cite>Kostyukova1995</cite>. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl <cite>Michael2014</cite>.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Kostyukova1995 pmid=7719281

#Brandi2009 pmid=18838391

#Luciane2002 pmid=12130645

#Daniel2003 pmid=12833544

#Alisdair2004 pmid=15214846

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-11-08T14:06:42Z

Menghui Sun:

{{CuratorApproved}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of the repeating disaccharide unit β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Michael2014 Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl [{{PDBlink}}4D0Q 4D0Q]. The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of the β-sheets.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus, such as Hyl from the PL8 family <cite>Daniel2003 Brandi2009</cite>. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix <cite>Alisdair2004</cite>. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread <cite>Luciane2002</cite>. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified: The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl.
;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930

#Kostyukova1995 pmid=7719281

#Brandi2009 pmid=18838391

#Luciane2002 pmid=12130645

#Daniel2003 pmid=12833544

#Alisdair2004 pmid=15214846

</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

Carbohydrate Binding Module Family 70

2024-10-30T05:39:08Z

Menghui Sun:

{{UnderConstruction}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of repeating disaccharide units of β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Michael2014 Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from ''S. pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl (PDB ID: 4D0Q). The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of β-sheet.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix. Infection by pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified
The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl.
;First Structural Characterization
The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

User:Menghui Sun

2024-10-30T03:15:15Z

Menghui Sun:

[[File:2.jpg|frameless|right]]
Menghui Sun is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. His research focuses on the rational design and application of carbohydrate-binding modules<cite>Xuanwei2022</cite>.

== References ==
<biblio>
#Xuanwei2022 pmid=36395930

</biblio>


[[Category:Contributors|Sun,Menghui]]

File:2.jpg

2024-10-30T03:10:08Z

Menghui Sun:

photo

File:SMH2.jpg

2024-10-30T02:57:01Z

Menghui Sun:

photo

User:Menghui Sun

2024-10-30T02:54:30Z

Menghui Sun:

[[File:SMH1.jpg|thumb]]
Menghui Sun is currently a Ph.D. student at the College of Food Science and Engineering, Ocean University of China, under the instruction of Prof. Yaoguang Chang. His research focuses on the rational design and application of carbohydrate-binding modules.

----

<biblio>
#Xuanwei2022 pmid=36395930

</biblio>


[[Category:Contributors|Sun,Menghui]]

User:Menghui Sun

2024-10-30T02:48:16Z

Menghui Sun:

[[File:SMH1.jpg|thumb]]
'''This is an empty template to help you get started with composing your User page.'''

You should begin by opening this page for editing by clicking on the Edit tab above. Your biography goes in this area of the page.

* See [[User:Gerlind_Sulzenbacher]] for an example. You may copy text from this example by opening the page in another browser window and clicking the "Edit" tab.
* Add your publications in the list below using PubMed IDs and cite them in the text like this <cite>Gilbert2008</cite>.
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''More specific help on these steps is available from the links under the "For contributors" section of the left page menu.''

----

<biblio>
#Gilbert2008 pmid=18430603

</biblio>


[[Category:Contributors|Sun,Menghui]]

File:SMH1.jpg

2024-10-30T02:48:07Z

Menghui Sun:

PHOTO

File:SMH.jpg

2024-10-30T02:44:14Z

Menghui Sun:

ID photo

Carbohydrate Binding Module Family 70

2024-10-30T02:33:03Z

Menghui Sun:

{{UnderConstruction}}
* [[Author]]: [[User:Menghui Sun|Menghui Sun]]
* [[Responsible Curator]]: [[User:Yaoguang Chang|Yaoguang Chang]]
----


<div style="float:right">
{| {{Prettytable}}
|-
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
|-
| colspan="2" |{{CAZyDBlink}}CBM70.html
|}
</div>


== Ligand specificities ==
The CBM70 family comprises members predominantly of bacterial origin. Notably, it is the only known family with a specific binding affinity for hyaluronic acid, a linear glycosaminoglycan composed of repeating disaccharide units of β-1,4-ᴅ-glucuronic acid-β-1,3-N-acetyl-ᴅ-glucosamine. Studies have shown that CBM70 modules typically do not bind to other glycosaminoglycans, such as chondroitin sulfate, dermatan sulfate, or heparin <cite>Michael2014 Xuanwei2022</cite>.

== Structural Features ==
CBM70 modules are typically composed of approximately 160 amino acids. The crystal structure of the N-terminal CBM70 module (SpCBM70) from ''S. pneumoniae'' hyaluronate lyase Hyl has been determined. SpCBM70 adopts a classic β-jelly roll fold, consisting of two opposing 5-stranded antiparallel β-sheets. This slightly bowed sandwich structure creates a groove along the concave surface, which carries a significant positive charge and is highly conserved within the CBM70 family <cite>Michael2014</cite>.[[File:CBM70.png|thumb|'''Figure 1.''' The fold of the hyaluronic acid binding molecule SpCBM70 from the ''Streptococcus pneumoniae'' hyaluronate lyase Hyl (PDB ID: 4D0Q). The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of β-sheet.]]

== Functionalities ==
CBM70 domains are commonly found as accessory modules in hyaluronate lyases produced by bacteria of the ''Streptococcus'' genus. These domains enhance the enzyme capability to degrade hyaluronic acid, a crucial component of the host's extracellular matrix. During infection, pathogens such as ''S. pneumoniae'' utilize hyaluronate lyase to break down hyaluronic acid, facilitating bacterial invasion and spread. CBM70 domains boost this process by increasing the binding efficiency of the enzyme, playing a key role in pathogen virulence and contributing to the high specificity of the enzyme for hyaluronic acid. Additionally, CBM70 domains have been effectively utilized in lateral flow immunoassays for the specific detection of hyaluronic acid, demonstrating their potential in diagnostic applications <cite>Xuanwei2022</cite>.

== Family Firsts ==
;First Identified
The first CBM70 module to be identified (SpCBM70) was from the ''S. pneumoniae'' hyaluronate lyase Hyl.
;First Structural Characterization
The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q.

== References ==
<biblio>
#Michael2014 pmid=25100731

#Xuanwei2022 pmid=36395930
</biblio>


[[Category:Carbohydrate Binding Module Families|CBM70]]

File:CBM70.png

2024-10-30T02:06:43Z

Menghui Sun:

Figure 1. The fold of the hyaluronic acid binding molecule SpCBM70 from the Streptococcus pneumoniae hyaluronate lyase Hyl (PDB ID: 4D0Q). The structure is rotated 90 degrees to illustrate the overall fold and the arrangement of β-sheet.