1bxw | pdb_00001bxw

OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN

spinqualitylabelsall models 1bxw, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bxw is a 1 chain structure with sequence from Escherichia coli bl21(de3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C8E Gene: OMPA (Escherichia coli BL21(DE3)) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1-171, by X-ray diffraction analysis, to a resolution of 2.5 A. It consists of a regular, extended eight-stranded beta-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane. Structure of the outer membrane protein A transmembrane domain.,Pautsch A, Schulz GE Nat Struct Biol. 1998 Nov;5(11):1013-7. PMID:9808047 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Homology modeling servers

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