2mpw

Solution structure of the LysM region of the E. coli Intimin periplasmic domainSolution structure of the LysM region of the E. coli Intimin periplasmic domain

Structural highlights 2mpw is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EAE_ECO27 Necessary for the production of attaching and effacing lesions on tissue culture cells. Believed to mediate adherence. Publication Abstract from PubMed Intimin and Invasin are prototypical inverse (Type Ve) autotransporters and important virulence factors of enteropathogenic Escherichia coli and Yersinia spp., respectively. In addition to a C-terminal extracellular domain and a beta-barrel transmembrane domain, both proteins also contain a short N-terminal periplasmic domain that, in Intimin, includes a lysin motif (LysM), which is thought to mediate binding to peptidoglycan. We show that the periplasmic domain of Intimin does bind to peptidoglycan both in vitro and in vivo, but only under acidic conditions. We were able to determine a dissociation constant of 0.8 muM for this interaction, whereas the Invasin periplasmic domain, which lacks a LysM, bound only weakly in vitro and failed to bind peptidoglycan in vivo. We present the solution structure of the Intimin LysM, which has an additional alpha-helix conserved within inverse autotransporter LysMs but lacking in others. In contrast to previous reports, we demonstrate that the periplasmic domain of Intimin mediates dimerisation. We further show that dimerisation and peptidoglycan binding are general features of LysM-containing inverse autotransporters. Peptidoglycan binding by the periplasmic domain in the infection process may aid in resisting mechanical and chemical stress during transit through the gastrointestinal tract. The Intimin periplasmic domain mediates dimerisation and binding to peptidoglycan.,Leo JC, Oberhettinger P, Chaubey M, Schutz M, Kuhner D, Bertsche U, Schwarz H, Gotz F, Autenrieth IB, Coles M, Linke D Mol Microbiol. 2014 Oct 29. doi: 10.1111/mmi.12840. PMID:25353290 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2mpw Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image