2km7 | pdb_00002km7

Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli

spinqualitylabelsall models 2km7, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2km7 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential beta-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex. Structure and function of BamE within the outer membrane and the beta-barrel assembly machine.,Knowles TJ, Browning DF, Jeeves M, Maderbocus R, Rajesh S, Sridhar P, Manoli E, Emery D, Sommer U, Spencer A, Leyton DL, Squire D, Chaudhuri RR, Viant MR, Cunningham AF, Henderson IR, Overduin M EMBO Rep. 2011 Feb 1;12(2):123-8. Epub 2011 Jan 7. PMID:21212804 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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