2v73: Difference between revisions
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<StructureSection load='2v73' size='340' side='right'caption='[[2v73]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2v73' size='340' side='right'caption='[[2v73]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v73]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2v73]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V73 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v73 OCA], [https://pdbe.org/2v73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v73 RCSB], [https://www.ebi.ac.uk/pdbsum/2v73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v73 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2YT71_CLOP1 A0A0H2YT71_CLOP1] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Clostridium perfringens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Boraston | [[Category: Boraston AB]] | ||
[[Category: Ficko-Blean | [[Category: Ficko-Blean E]] | ||
[[Category: Healey | [[Category: Healey M]] | ||
Latest revision as of 12:55, 9 May 2024
The structure of the family 40 CBM from C. perfringens NanJ in complex with a sialic acid containing moleculeThe structure of the family 40 CBM from C. perfringens NanJ in complex with a sialic acid containing molecule
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMyonecrotic isolates of Clostridium perfringens secrete multimodular sialidases, often termed "large sialidases", that contribute to the virulence of this bacterium. NanJ is the largest of the two secreted sialidases at 1173 amino acids and comprises 6 different modules which are, from the N-terminus, a family 32 carbohydrate binding module (CBM), a family 40 CBM, a family 33 glycoside hydrolase, a module of unknown function, a family 82 "X-module" of unknown function, and a module with amino acid similarity to fibronectin type III domains. The hydrolase activity of clostridial sialidases is quite well documented; however, the functions of their accessory domains are entirely uninvestigated. Here we describe the carbohydrate binding activity of the isolated family 32 CBM (CBM32) and the isolated family 40 CBM (CBM40). CBM32 is shown to bind galactose or N-acetylgalactosamine, while CBM40 is sialic acid specific, though both CBMs appear to bind with very low affinities. The crystal structure of CBM32 was determined at 2.25 A in complex with galactose. This revealed what appears to be a very simple galactose binding site. The crystal structure of CBM40 was determined at 2.20 A in complex with a sialic acid containing molecule that it fortuitously crystallized with, revealing the molecular details of the CBM40-sialic acid interaction. Overall, the results indicate that NanJ contains carbohydrate specific binding modules that likely function to target the enzyme to molecules or cells bearing mixed populations of glycans that terminate in either galactose/N-acetylgalactosamine or sialic acid. Carbohydrate recognition by a large sialidase toxin from Clostridium perfringens.,Boraston AB, Ficko-Blean E, Healey M Biochemistry. 2007 Oct 9;46(40):11352-60. Epub 2007 Sep 13. PMID:17850114[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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