4x4a: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with 2,7-Anhydro-Neu5Ac==
<StructureSection load='4x4a' size='340' side='right' caption='[[4x4a]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


The entry 4x4a is ON HOLD  until Paper Publication
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>


Authors: Owen, C.D., Tailford, L.E., Taylor, G.L., Juge, N.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description:
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Owen, C.D]]
__TOC__
[[Category: Taylor, G.L]]
</StructureSection>
[[Category: Tailford, L.E]]
[[Category: Juge, N]]
[[Category: Juge, N]]
[[Category: Owen, C D]]
[[Category: Tailford, L E]]
[[Category: Taylor, G L]]
[[Category: 2-7-anhydro-neu5ac]]
[[Category: Anhydrosialdiase]]
[[Category: Hydrolase]]
[[Category: Intramolecular]]
[[Category: Neuraminidase]]
[[Category: Reaction product]]
[[Category: Sialidase]]
[[Category: Trans-sialidase]]
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