We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
4x6k
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B== |
| + | <StructureSection load='4x6k' size='340' side='right' caption='[[4x6k]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4x6k]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X6K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X6K FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3XR:(2S,3R,4S,5S)-2-(ACETYLAMINO)-5-CARBOXY-3,4-DIHYDROXYPIPERIDINIUM'>3XR</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</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=4x6k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x6k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x6k RCSB], [http://www.ebi.ac.uk/pdbsum/4x6k 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 >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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
[[Category: Juge, N]] | [[Category: Juge, N]] | ||
| + | [[Category: Owen, C D]] | ||
| + | [[Category: Tailford, L E]] | ||
| + | [[Category: Taylor, G L]] | ||
| + | [[Category: Anhydrosialidase]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Inhibitor]] | ||
| + | [[Category: Intramolecular]] | ||
| + | [[Category: Neuraminidase]] | ||
| + | [[Category: Sialidase]] | ||
| + | [[Category: Siastatin b]] | ||
| + | [[Category: Trans-sialidase]] | ||
Revision as of 14:06, 22 July 2015
Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Siastatin B
| |||||||||||
