2K0L
NMR structure of the transmembrane domain of the Outer Membrane Protein A from Klebsiella pneumoniae in DHPC micelles.
Summary for 2K0L
| Entry DOI | 10.2210/pdb2k0l/pdb |
| NMR Information | BMRB: 15651 |
| Descriptor | Outer membrane protein A (1 entity in total) |
| Functional Keywords | ompa, membrane protein, trosy, sidechain, dhpc micelles |
| Biological source | Klebsiella pneumoniae |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P24017 |
| Total number of polymer chains | 1 |
| Total formula weight | 23394.81 |
| Authors | Renault, M.,Saurel, O.,Gervais, V.,Lohr, F.,Reat, V.,Piotto, M.,Milon, A. (deposition date: 2008-02-04, release date: 2008-12-23, Last modification date: 2024-05-29) |
| Primary citation | Renault, M.,Saurel, O.,Czaplicki, J.,Demange, P.,Gervais, V.,Lohr, F.,Reat, V.,Piotto, M.,Milon, A. Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications. J.Mol.Biol., 385:117-130, 2009 Cited by PubMed Abstract: 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). PubMed: 18952100DOI: 10.1016/j.jmb.2008.10.021 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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