7lbv

Crystal structure of the Propionibacterium acnes surface sialidase in complex with Neu5Ac2en

spinqualitylabelsall models 7lbv, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: DAN, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Propionibacterium acnes, though generally considered part of the normal flora of human skin, is an opportunistic pathogen associated with acne vulgaris as well as other diseases, including endocarditis, endophthalmitis and prosthetic joint infections. Its virulence potential is also supported by knowledge gained from its sequenced genome. Indeed, a vaccine targeting a putative cell wall-anchored P. acnes sialidase has been shown to suppress cytotoxicity and pro-inflammatory cytokine release induced by the organism, and is proposed as an alternative treatment for P. acnes-associated diseases. Here, we report the crystal structures of the surface sialidase and its complex with the transition-state mimic Neu5Ac2en. Our structural and kinetic analyses, together with insight from a glycan array screen, which probes subtle specificities of the sialidase for alpha-2,3-sialosides, provide a basis for the structure-based design of novel small-molecule therapeutics against P. acnes infections. Crystal structure of the Propionibacterium acnes surface sialidase, a drug target for P. acnes-associated diseases.,Yu ACY, Volkers G, Jongkees SAK, Worrall LJ, Withers SG, Strynadka NCJ Glycobiology. 2021 Nov 17. pii: 6430129. doi: 10.1093/glycob/cwab094. PMID:34792586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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