1g90

NMR Solution Structure of Outer Membrane Protein A Transmembrane Domain: 10 conformers

spinqualitylabelsall models 1g90 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1g90 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 OMPA_ECOLI Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes. 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 We have determined the three-dimensional fold of the 19 kDa (177 residues) transmembrane domain of the outer membrane protein A of Escherichia coli in dodecylphosphocholine (DPC) micelles in solution using heteronuclear NMR. The structure consists of an eight-stranded beta-barrel connected by tight turns on the periplasmic side and larger mobile loops on the extracellular side. The solution structure of the barrel in DPC micelles is similar to that in n-octyltetraoxyethylene (C(8)E(4)) micelles determined by X-ray diffraction. Moreover, data from NMR dynamic experiments reveal a gradient of conformational flexibility in the structure that may contribute to the membrane channel function of this protein. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.,Arora A, Abildgaard F, Bushweller JH, Tamm LK Nat Struct Biol. 2001 Apr;8(4):334-8. PMID:11276254 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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