2mhl | pdb_00002mhl

NMR solution Structure of the E.coli Outer Membrane Protein W

spinqualitylabelsall models 2mhl, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mhl 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 The outer membrane proteins (Omps) are key factors for bacterial survival and virulence. Among the Omps that have been structurally characterized either by X-ray crystallography or by NMR in solution, the crystal structure of OmpW stands out because three of its four extracellular loops are well defined, whereas long extracellular loops in other E. coli Omps are disordered in the crystals as well as in NMR structures. OmpW thus presented an opportunity for a detailed comparison of the extracellular loops in a beta-barrel membrane protein structure in crystals and in noncrystalline milieus. Here, the polypeptide backbone conformation of OmpW in 30-Fos micelles was determined. Complete backbone NMR assignments were obtained and the loops were structurally characterized. In combination with the OmpW crystal structure, NMR line shape analyses, and 15N{1H}-NOE data, these results showed that intact regular secondary structures in the loops undergo slow hinge motions at the detergent-solvent interface. NMR Polypeptide Backbone Conformation of the E. coli Outer Membrane Protein W.,Horst R, Stanczak P, Wuthrich K Structure. 2014 Jul 9. pii: S0969-2126(14)00176-2. doi:, 10.1016/j.str.2014.05.016. PMID:25017731 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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