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| | <StructureSection load='4x47' size='340' side='right'caption='[[4x47]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4x47' size='340' side='right'caption='[[4x47]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4x47]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rumgv Rumgv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X47 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X47 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4x47]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminococcus_gnavus_ATCC_29149 Ruminococcus gnavus ATCC 29149]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X47 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF1201_01421 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=411470 RUMGV])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4x47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x47 OCA], [https://pdbe.org/4x47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x47 RCSB], [https://www.ebi.ac.uk/pdbsum/4x47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x47 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=4x47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x47 OCA], [http://pdbe.org/4x47 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x47 RCSB], [http://www.ebi.ac.uk/pdbsum/4x47 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x47 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Sialidase|Sialidase]] | + | *[[Neuraminidase 3D structures|Neuraminidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Exo-alpha-sialidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rumgv]]
| + | [[Category: Juge N]] |
| - | [[Category: Juge, N]] | + | [[Category: Owen CD]] |
| - | [[Category: Owen, C D]] | + | [[Category: Tailford LE]] |
| - | [[Category: Tailford, L E]] | + | [[Category: Taylor GL]] |
| - | [[Category: Taylor, G L]] | + | |
| - | [[Category: Anhydrosialidase]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Dana]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Inhibitor]]
| + | |
| - | [[Category: Intramolecular]]
| + | |
| - | [[Category: Neu5ac2en]]
| + | |
| - | [[Category: Neuraminidase]]
| + | |
| - | [[Category: Sialidase]]
| + | |
| - | [[Category: Trans-sialidase]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tailford LE, Owen CD, Walshaw J, Crost EH, Hardy-Goddard J, Le Gall G, de Vos WM, Taylor GL, Juge N. Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation. Nat Commun. 2015 Jul 8;6:7624. doi: 10.1038/ncomms8624. PMID:26154892 doi:http://dx.doi.org/10.1038/ncomms8624
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