4X49
Crystal structure of the intramolecular trans-sialidase from Ruminococcus gnavus in complex with oseltamivir carboxylate
Summary for 4X49
| Entry DOI | 10.2210/pdb4x49/pdb |
| Descriptor | Anhydrosialidase, (3R,4R,5S)-4-(acetylamino)-5-amino-3-(pentan-3-yloxy)cyclohex-1-ene-1-carboxylic acid, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | intramolecular, trans-sialidase, sialidase, neuraminidase, oseltamivir carboxylate, tamiflu, inhibitor, complex, hydrolase, anhydrosialidase |
| Biological source | Ruminococcus gnavus ATCC 29149 |
| Total number of polymer chains | 1 |
| Total formula weight | 54817.57 |
| Authors | Owen, C.D.,Tailford, L.E.,Taylor, G.L.,Juge, N. (deposition date: 2014-12-02, release date: 2015-07-22, Last modification date: 2024-01-10) |
| Primary citation | Tailford, L.E.,Owen, C.D.,Walshaw, J.,Crost, E.H.,Hardy-Goddard, J.,Le Gall, G.,de Vos, W.M.,Taylor, G.L.,Juge, N. Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation. Nat Commun, 6:7624-7624, 2015 Cited by PubMed Abstract: 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 α2-3-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. PubMed: 26154892DOI: 10.1038/ncomms8624 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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