2k0l

NMR structure of the transmembrane domain of the Outer Membrane Protein A from Klebsiella pneumoniae in DHPC micelles.

spinqualitylabelsall models 2k0l Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k0l is a 1 chain structure with sequence from Klebsiella pneumoniae. 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_KLEPN 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 (By similarity). 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 three-dimensional structure of the outer membrane protein A from Klebsiella pneumoniae transmembrane domain was determined by NMR.This protein induces specific humoral and cytotoxic responses, and is a potent carrier protein. This is one of the largest integral membrane proteins(210 residues) for which nearly complete resonance assignment, including side chains, has been achieved so far. The methodology rested on the use of 900 MHz 3D and 4D TROSY experiments recorded on a uniformly 15N,13C,2H-labeled sample and on a perdeuterated methyl protonated sample. The structure was refined from 920 experimental constraints, giving an ensemble of 20 best structures with an r.m.s. deviation of 0.54 A for the main chain atoms in the core eight-stranded beta-barrel. The protein dynamics was assessed, in a residue-specific manner, by 1H-15N NOEs (pico- to nanosecond timescale), exchange broadening (millisecond to second) and 1H-2H chemical exchange (hour-weeks). Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications.,Renault M, Saurel O, Czaplicki J, Demange P, Gervais V, Lohr F, Reat V, Piotto M, Milon A J Mol Biol. 2009 Jan 9;385(1):117-30. Epub 2008 Oct 15. PMID:18952100 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also C-X-C motif chemokine 3D structures Porin 3D structures Stromal Derived Factor 1

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