4x47: Difference between revisions

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==Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2en==
==Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2en==
<StructureSection load='4x47' size='340' side='right' caption='[[4x47]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4x47' size='340' side='right'caption='[[4x47]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4x47]] is a 1 chain structure. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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='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='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>
<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>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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</div>
</div>
<div class="pdbe-citations 4x47" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4x47" style="background-color:#fffaf0;"></div>
==See Also==
*[[Neuraminidase 3D structures|Neuraminidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Exo-alpha-sialidase]]
[[Category: Large Structures]]
[[Category: Juge, N]]
[[Category: Juge N]]
[[Category: Owen, C D]]
[[Category: Owen CD]]
[[Category: Tailford, L E]]
[[Category: Tailford LE]]
[[Category: Taylor, G L]]
[[Category: Taylor GL]]
[[Category: Anhydrosialidase]]
[[Category: Complex]]
[[Category: Dana]]
[[Category: Hydrolase]]
[[Category: Inhibitor]]
[[Category: Intramolecular]]
[[Category: Neu5ac2en]]
[[Category: Neuraminidase]]
[[Category: Sialidase]]
[[Category: Trans-sialidase]]

Latest revision as of 13:46, 10 January 2024

Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2enCrystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with Neu5Ac2en

Structural highlights

4x47 is a 1 chain structure with sequence from Ruminococcus gnavus ATCC 29149. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

4x47, resolution 2.00Å

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