2K0L

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

2K0L の概要

• エントリーDOI: 10.2210/pdb2k0l/pdb
• NMR情報: BMRB: 15651
• 分子名称: Outer membrane protein A (1 entity in total)
• 機能のキーワード: ompa, membrane protein, trosy, sidechain, dhpc micelles
• 由来する生物種: Klebsiella pneumoniae
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P24017
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23394.81

構造登録者

Renault, M.,Saurel, O.,Gervais, V.,Lohr, F.,Reat, V.,Piotto, M.,Milon, A. (登録日: 2008-02-04, 公開日: 2008-12-23, 最終更新日: 2024-05-29)

主引用文献

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

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: 18952100
DOI: 10.1016/j.jmb.2008.10.021

実験手法

SOLUTION NMR