4kku

Structure of BesA (Selenomethinone derivative - P212121)

spinqualitylabelsall models 4kku, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kku is a 4 chain structure with sequence from Borreliella burgdorferi B31. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O51166_BORBU Publication Abstract from PubMed Periplasmic adaptor proteins are essential components of bacterial tripartite multidrug efflux pumps. Here we report the 2.35A resolution crystal structure of the BesA adaptor from the spirochete Borrelia burgdorferi solved using selenomethionine derivatized protein. BesA shows the archetypal linear, flexible, multi-domain architecture evident among proteobacteria and retains the lipoyl, beta-barrel and membrane-proximal domains that interact with the periplasmic domains of the inner membrane transporter. However, it lacks the alpha-hairpin domain shown to establish extensive coiled-coil interactions with the periplasmic entrance helices of the outer membrane-anchored TolC exit duct. This has implications for the modelling of assembled tripartite efflux pumps. Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi.,Greene NP, Hinchliffe P, Crow A, Ababou A, Hughes C, Koronakis V FEBS Lett. 2013 Jul 9. pii: S0014-5793(13)00520-6. doi:, 10.1016/j.febslet.2013.06.056. PMID:23851070 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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