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2w1s

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Revision as of 21:23, 19 September 2018

Unique ligand binding specificity of a family 32 Carbohydrate-Binding Module from the Mu toxin produced by Clostridium perfringens

Structural highlights

2w1s is a 2 chain structure with sequence from "bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	2w1q, 2w1u, 2wdb
Activity:	Hydrolase, with EC number 3.2.1.35
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Many carbohydrate-active enzymes have complex architectures comprising multiple modules that may be involved in catalysis, carbohydrate binding, or protein-protein interactions. Carbohydrate-binding modules (CBMs) are a common ancillary module whose function is to promote the adherence of the complete enzyme to carbohydrate substrates. CBM family 32 has been proposed to be one of the most diverse CBM families classified to date, yet all of the structurally characterized CBM32s thus far recognize galactose-based ligands. Here, we report a unique binding specificity and mode of ligand binding for a family 32 CBM. NagHCBM32-2 is one of four CBM32 modules in NagH, a family 84 glycoside hydrolase secreted by Clostridium perfringens. NagHCBM32-2 has the beta-sandwich scaffold common to members of the family; however, its specificity for N-acetylglucosamine is unusual among CBMs. X-ray crystallographic analysis of the module at resolutions from 1.45 to 2.0 A and in complex with disaccharides reveals that its mode of sugar recognition is quite different from that observed for galactose-specific CBM32s. This study continues to unravel the diversity of CBMs found in family 32 and how these CBMs might impart the carbohydrate-binding specificity to the extracellular glycoside hydrolases in C. perfringens.

N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH.,Ficko-Blean E, Boraston AB J Mol Biol. 2009 Jul 10;390(2):208-20. Epub 2009 May 5. PMID:19422833^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ficko-Blean E, Boraston AB. N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH. J Mol Biol. 2009 Jul 10;390(2):208-20. Epub 2009 May 5. PMID:19422833 doi:10.1016/j.jmb.2009.04.066

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w1s"

@@ Line 1: / Line 1: @@
-==UNIQUE LIGAND BINDING SPECIFICITY OF A FAMILY 32 CARBOHYDRATE-BINDING MODULE FROM THE MU TOXIN PRODUCED BY CLOSTRIDIUM PERFRINGENS==
+==Unique ligand binding specificity of a family 32 Carbohydrate-Binding Module from the Mu toxin produced by Clostridium perfringens==
 <StructureSection load='2w1s' size='340' side='right' caption='[[2w1s]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w1q|2w1q]], [[2w1u|2w1u]], [[2wdb|2wdb]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w1s OCA], [http://pdbe.org/2w1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w1s RCSB], [http://www.ebi.ac.uk/pdbsum/2w1s PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w1s OCA], [http://pdbe.org/2w1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w1s RCSB], [http://www.ebi.ac.uk/pdbsum/2w1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w1s ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w1/2w1s_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w1/2w1s_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2w1s

From Proteopedia

Revision as of 21:23, 19 September 2018

Unique ligand binding specificity of a family 32 Carbohydrate-Binding Module from the Mu toxin produced by Clostridium perfringens

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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