Difference between revisions of "Carbohydrate Binding Module Family 100"

Latest revision as of 01:40, 16 February 2024

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Ligand specificities

Figure 1. Domain analysis of the parent enzyme of PhCBM100.The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids)[].

The first characterized member of the CBM100 family, PhCBM100[1], was found in a PL29 putative chondroitin lyase from Polaribacter haliotis. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber Apostichopus japonicus, whereas it was incapable of binding to other glycosaminoglycans or polyuronic acids. PhCBM100 displays high affinity for CS-A and CS-C with the K_a values of 2.1×10⁶ M^-1 and 6.0×10⁶ M^-1, respectively, as demonstrated by affinity electrophoresis assays [1].

Structural Features

Figure 2. Structure of PhCBM100. (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge) [].

The 1.55 Å resolution X-ray crystal structure of PhCBM100 (PDB 8jiy) exhibited a β-sandwich fold formed of 10 β-strands and 2 helices[1]. A groove with both a distinct overall positive charge and a high degree of conserved residues is proposed as the binding site, it is enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through ionic contacts[1].

Functionalities

PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The in situ visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein[1].

Family Firsts

First Identified: The chondroitin sulfate binding PhCBM100 from the P. haliotis PL29 putative chondroitin lyase was the first member of the family to be identified and characterized[1].
First Structural Characterization: PhCBM100 was the first structurally characterized CBM100[1].

References

Liu G, Chang Y, Mei X, Chen G, Zhang Y, Jiang X, Tao W, and Xue C. (2024). Identification and structural characterization of a novel chondroitin sulfate-specific carbohydrate-binding module: The first member of a new family, CBM100. Int J Biol Macromol. 2024;255:127959. DOI:10.1016/j.ijbiomac.2023.127959 | PubMed ID:37951443 [Liu2023]

@@ Line 1: / Line 1: @@
 <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
-{{UnderConstruction}}
+{{CuratorApproved}}
 * [[Author]]: [[User:Guanchen Liu|Guanchen Liu]]
 * [[Responsible Curator]]:  [[User:Yaoguang Chang|Yaoguang Chang]]
@@ Line 18: / Line 18: @@
 == Ligand specificities ==
-[[File:Fig.1 300.png|thumb|300px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a PL29 domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids).]]
+[[File:Fig.1 300.png|thumb|250px|right|'''Figure 1. Domain analysis of the parent enzyme of PhCBM100.'''The enzyme consists of a signal peptide (1-23 amino acids), a [[PL29]] domain (68-399 amino acids), a CBM100 domain (viz., PhCBM100; 555-785 amino acids) and a C-terminal sorting domain (786-851 amino acids)<cite>Liu2023</cite>.]]
-The first characterized member of the CBM100 family, PhCBM100<cite>Liu2024</cite>, was found in a PL29 putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas incapable of binding to other glycosaminoglycans or polyuronic acids. By affinity electrophoresis assays, PhCBM100 displays high affinity for CS-A and CS-C with the Ka values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively.
+The first characterized member of the CBM100 family, PhCBM100<cite>Liu2023</cite>, was found in a [[PL29]] putative chondroitin lyase from ''Polaribacter haliotis''. PhCBM100 bound specifically to chondroitin sulfates (CSs) including CS-A, CS-C and fucosylated chondroitin sulfate from sea cucumber ''Apostichopus japonicus'', whereas it was incapable of binding to other glycosaminoglycans or polyuronic acids.  PhCBM100 displays high affinity for CS-A and CS-C with the ''K''<sub>a</sub> values of 2.1×10<sup>6</sup> M<sup>-1</sup> and 6.0×10<sup>6</sup> M<sup>-1</sup>, respectively, as demonstrated by affinity electrophoresis assays <cite>Liu2023</cite>.
 == Structural Features ==
-[[File:Fig.2 300.png|thumb|600px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge).]]
+[[File:Fig.2 300.png|thumb|400px|right|'''Figure 2. Structure of PhCBM100.''' (A) Schematic representation of PhCBM100 showing helices in yellow and strands in cyan. (B) Detailed view of the putative PhCBM100 binding site. The surface is colored by electrostatic potential, from blue (positive charge) to red (negative charge) <cite>Liu2023</cite>.]]
-The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed by two antiparallel comprised of 10 β-strands and 2 helices.
+The 1.55 Å resolution X-ray crystal structure of PhCBM100 ([{{PDBlink}}8jiy PDB 8jiy]) exhibited a β-sandwich fold formed  of 10 β-strands and 2 helices<cite>Liu2023</cite>.
-A groove with both a distinct positive charge and a high degree of conserved residues is proposed as the binding site, enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through the ionic contacts.
+A groove with both a distinct overall positive charge and a high degree of conserved residues is proposed as the binding site, it is enriched with hydrophilic amino acids. As the result of molecular docking, the basic amino acid residues (e.g., Lys-40, Arg-122 and Arg-201) of PhCBM100 may contribute to CS binding through ionic contacts<cite>Liu2023</cite>.
 == Functionalities ==
-PhCBM100 is a component of a PL29 enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein.
+PhCBM100 is a component of a [[PL29]] enzyme that displays chondroitin-sulfate ABC endolyase activity, consistent with the PhCBM100 specificity. The ''in situ'' visualization of chondroitin sulfate in animal tissues (e.g., chicken cartilage, bovine muscle, and porcine laryngeal cartilage) was realized by utilizing a fluorescent probe constructed by fusing PhCBM100 with a green fluorescent protein<cite>Liu2023</cite>.
 == Family Firsts ==
-;First Identified:The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' PL29 putative chondroitin lyase was the first member of the family to be identified and characterized.
+;First Identified: The chondroitin sulfate binding PhCBM100 from the ''P. haliotis'' [[PL29]] putative chondroitin lyase was the first member of the family to be identified and characterized<cite>Liu2023</cite>.
-;First Structural Characterization:PhCBM100 was also the first structurally characterized CBM100.
+;First Structural Characterization: PhCBM100 was the first structurally characterized CBM100<cite>Liu2023</cite>.
 == References ==
 <biblio>
-#Liu2024 pmid=37951443
+#Liu2023 pmid=37951443
 </biblio>
 <!-- Do not delete this Category tag -->
 [[Category:Carbohydrate Binding Module Families|CBM100]]