2v5c: Difference between revisions
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==Family 84 glycoside hydrolase from Clostridium perfringens, 2.1 Angstrom structure== | |||
<StructureSection load='2v5c' size='340' side='right' caption='[[2v5c]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2v5c' size='340' side='right' caption='[[2v5c]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j62|2j62]], [[2jh2|2jh2]], [[2vur|2vur]], [[2v5d|2v5d]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j62|2j62]], [[2jh2|2jh2]], [[2vur|2vur]], [[2v5d|2v5d]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=2v5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5c OCA], [http://pdbe.org/2v5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v5c RCSB], [http://www.ebi.ac.uk/pdbsum/2v5c 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=2v5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5c OCA], [http://pdbe.org/2v5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v5c RCSB], [http://www.ebi.ac.uk/pdbsum/2v5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/2v5c_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/2v5c_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Carbohydrate binding module]] | [[Category: Carbohydrate binding module]] | ||
[[Category: Clostridium perfringen]] | [[Category: Clostridium perfringen]] | ||
[[Category: Coiled coil]] | |||
[[Category: Family 84 glycoside hydrolase]] | [[Category: Family 84 glycoside hydrolase]] | ||
[[Category: Gh84]] | [[Category: Gh84]] | ||
Revision as of 11:26, 12 September 2018
Family 84 glycoside hydrolase from Clostridium perfringens, 2.1 Angstrom structureFamily 84 glycoside hydrolase from Clostridium perfringens, 2.1 Angstrom structure
Structural highlights
Function[OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. 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 PubMedCommon features of the extracellular carbohydrate-active virulence factors involved in host-pathogen interactions are their large sizes and modular complexities. This has made them recalcitrant to structural analysis, and therefore our understanding of the significance of modularity in these important proteins is lagging. Clostridium perfringens is a prevalent human pathogen that harbors a wide array of large, extracellular carbohydrate-active enzymes and is an excellent and relevant model system to approach this problem. Here we describe the complete structure of C. perfringens GH84C (NagJ), a 1001-amino acid multimodular homolog of the C. perfringens micro-toxin, which was determined using a combination of small angle x-ray scattering and x-ray crystallography. The resulting structure reveals unprecedented insight into how catalysis, carbohydrate-specific adherence, and the formation of molecular complexes with other enzymes via an ultra-tight protein-protein interaction are spatially coordinated in an enzyme involved in a host-pathogen interaction. Portrait of an enzyme, a complete structural analysis of a multimodular {beta}-N-acetylglucosaminidase from Clostridium perfringens.,Ficko-Blean E, Gregg KJ, Adams JJ, Hehemann JH, Czjzek M, Smith SP, Boraston AB J Biol Chem. 2009 Apr 10;284(15):9876-84. Epub 2009 Feb 4. PMID:19193644[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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