6er2 | pdb_00006er2

Ruminococcus gnavus IT-sialidase CBM40

spinqualitylabelsall models 6er2, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6er2 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Ruminococcus gnavus is a human gut symbiont wherein the ability to degrade mucins is mediated by an intramolecular trans-sialidase (RgNanH). RgNanH comprises a GH33 catalytic domain and a sialic acid-binding carbohydrate-binding module (CBM40). Here we used glycan arrays, STD NMR, X-ray crystallography, mutagenesis and binding assays to determine the structure and function of RgNanH_CBM40 (RgCBM40). RgCBM40 displays the canonical CBM40 beta-sandwich fold and broad specificity towards sialoglycans with millimolar binding affinity towards alpha2,3- or alpha2,6-sialyllactose. RgCBM40 binds to mucus produced by goblet cells and to purified mucins, providing direct evidence for a CBM40 as a novel bacterial mucus adhesin. Bioinformatics data show that RgCBM40 canonical type domains are widespread among Firmicutes. Furthermore, binding of R. gnavus ATCC 29149 to intestinal mucus is sialic acid mediated. Together, this study reveals novel features of CBMs which may contribute to the biogeography of symbiotic bacteria in the gut. Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus.,Owen CD, Tailford LE, Monaco S, Suligoj T, Vaux L, Lallement R, Khedri Z, Yu H, Lecointe K, Walshaw J, Tribolo S, Horrex M, Bell A, Chen X, Taylor GL, Varki A, Angulo J, Juge N Nat Commun. 2017 Dec 19;8(1):2196. doi: 10.1038/s41467-017-02109-8. PMID:29259165 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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