5vj8

Backbone structure of the Yersinia pestis outer membrane protein Ail in phospholipid bilayer nanodisc

spinqualitylabelsall models 5vj8, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vj8 is a 1 chain structure with sequence from "bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2n2l Gene: AVJ24_14645, AVO31_14870 ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Yersinia pestis the causative agent of plague, is highly pathogenic and poses very high risk to public health. The outer membrane protein Ail (Adhesion invasion locus) is one of the most highly expressed proteins on the cell surface of Y. pestis, and a major target for the development of medical countermeasures. Ail is essential for microbial virulence and is critical for promoting the survival of Y. pestis in serum. Structures of Ail have been determined by X-ray diffraction and solution NMR spectroscopy, but the protein's activity is influenced by the detergents in these samples, underscoring the importance of the surrounding environment for structure-activity studies. Here we describe the backbone structure of Ail, determined in lipid bilayer nanodiscs, using solution NMR spectroscopy. We also present solid-state NMR data obtained for Ail in membranes containing lipopolysaccharide (LPS), a major component of the bacterial outer membranes. The protein in lipid bilayers, adopts the same eight-stranded beta-barrel fold observed in the crystalline and micellar states. The membrane composition, however, appears to have a marked effect on protein dynamics, with LPS enhancing conformational order and slowing down the (15)N transverse relaxation rate. The results provide information about the way in which an outer membrane protein inserts and functions in the bacterial membrane. Structural Insights into the Yersinia pestis Outer Membrane Protein Ail in Lipid Bilayers.,Dutta SK, Yao Y, Marassi FM J Phys Chem B. 2017 Aug 17;121(32):7561-7570. doi: 10.1021/acs.jpcb.7b03941. Epub, 2017 Aug 4. PMID:28726410 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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