4x4a

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'''Unreleased structure'''
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==Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with 2,7-Anhydro-Neu5Ac==
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<StructureSection load='4x4a' size='340' side='right' caption='[[4x4a]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4x4a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X4A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X4A FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SKD:2-ACETYLAMINO-7-(1,2-DIHYDROXY-ETHYL)-3-HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCTANE-5-CARBOXYLIC+ACID'>SKD</scene></td></tr>
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<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=4x4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x4a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x4a RCSB], [http://www.ebi.ac.uk/pdbsum/4x4a PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The gastrointestinal mucus layer is colonized by a dense community of microbes catabolizing dietary and host carbohydrates during their expansion in the gut. Alterations in mucosal carbohydrate availability impact on the composition of microbial species. Ruminococcus gnavus is a commensal anaerobe present in the gastrointestinal tract of &gt;90% of humans and overrepresented in inflammatory bowel diseases (IBD). Using a combination of genomics, enzymology and crystallography, we show that the mucin-degrader R. gnavus ATCC 29149 strain produces an intramolecular trans-sialidase (IT-sialidase) that cleaves off terminal alpha2-3-linked sialic acid from glycoproteins, releasing 2,7-anhydro-Neu5Ac instead of sialic acid. Evidence of IT-sialidases in human metagenomes indicates that this enzyme occurs in healthy subjects but is more prevalent in IBD metagenomes. Our results uncover a previously unrecognized enzymatic activity in the gut microbiota, which may contribute to the adaptation of intestinal bacteria to the mucosal environment in health and disease.
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The entry 4x4a is ON HOLD until Paper Publication
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Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation.,Tailford LE, Owen CD, Walshaw J, Crost EH, Hardy-Goddard J, Le Gall G, de Vos WM, Taylor GL, Juge N Nat Commun. 2015 Jul 8;6:7624. doi: 10.1038/ncomms8624. PMID:26154892<ref>PMID:26154892</ref>
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Authors: Owen, C.D., Tailford, L.E., Taylor, G.L., Juge, N.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description:
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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[[Category: Owen, C.D]]
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__TOC__
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[[Category: Taylor, G.L]]
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</StructureSection>
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[[Category: Tailford, L.E]]
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[[Category: Juge, N]]
[[Category: Juge, N]]
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[[Category: Owen, C D]]
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[[Category: Tailford, L E]]
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[[Category: Taylor, G L]]
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[[Category: 2-7-anhydro-neu5ac]]
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[[Category: Anhydrosialdiase]]
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[[Category: Hydrolase]]
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[[Category: Intramolecular]]
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[[Category: Neuraminidase]]
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[[Category: Reaction product]]
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[[Category: Sialidase]]
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[[Category: Trans-sialidase]]

Revision as of 14:10, 22 July 2015

Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with 2,7-Anhydro-Neu5Ac

4x4a, resolution 1.71Å

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