Carbohydrate Binding Module Family 70 - Revision history

Elizabeth Ficko-Blean at 13:13, 30 October 2025

2025-10-30T13:13:42Z

Menghui Sun at 03:21, 13 November 2024

2024-11-13T03:21:11Z

Menghui Sun at 09:11, 10 November 2024

2024-11-10T09:11:16Z

Menghui Sun at 09:10, 10 November 2024

2024-11-10T09:10:42Z

Menghui Sun at 09:08, 10 November 2024

2024-11-10T09:08:30Z

Menghui Sun at 14:15, 8 November 2024

2024-11-08T14:15:35Z

Menghui Sun at 14:13, 8 November 2024

2024-11-08T14:13:41Z

Menghui Sun at 14:11, 8 November 2024

2024-11-08T14:11:46Z

Menghui Sun at 14:06, 8 November 2024

2024-11-08T14:06:42Z

Elizabeth Ficko-Blean: /* Ligand specificities */

2024-11-06T15:22:24Z

Ligand specificities

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 <!-- Do not delete this Category tag -->
-[[Category:Carbohydrate Binding Module Families|CBM70]]
+[[Category:Carbohydrate Binding Module Families|CBM070]]
 <!-- ATTENTION: Make sure to replace "nnn" with a three digit family number, e.g. "032" or "105" etc., for proper sorting of the page by family number. -->

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 == 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>.
+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 ==

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 #Xuanwei2022 pmid=36395930
-#Alisdair2002 pmid:12079353
+#Alisdair2002 pmid=12079353
 #Daniel2003 pmid=12833544

@@ Line 20: / Line 20: @@
 == 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>.]]
+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 ==
@@ Line 34: / Line 34: @@
 #Xuanwei2022 pmid=36395930
 #Daniel2003 pmid=12833544

@@ Line 20: / Line 20: @@
 == 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>.]]
+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 ==

@@ Line 17: / Line 17: @@
 == 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>.
+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 ==

@@ Line 20: / Line 20: @@
 == 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.]]
+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. 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>.
+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.
+;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.
+;First Structural Characterization: The first crystal structure of a CBM70 module was also that of SpCBM70, PDB ID 4D0Q <cite>Michael2014</cite>.
 == References ==