1G90

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

1G90 の概要

• エントリーDOI: 10.2210/pdb1g90/pdb
• 関連するPDBエントリー: 1QJP
• 分子名称: OUTER MEMBRANE PROTEIN A (1 entity in total)
• 機能のキーワード: beta barrel, integral membrane protein, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P0A910
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19060.98

構造登録者

Arora, A.,Abildgaard, F.,Bushweller, J.H.,Tamm, L.K. (登録日: 2000-11-21, 公開日: 2001-04-21, 最終更新日: 2024-05-22)

主引用文献

Arora, A.,Abildgaard, F.,Bushweller, J.H.,Tamm, L.K.
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
Nat.Struct.Biol., 8:334-338, 2001

PubMed Abstract: 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.

PubMed: 11276254
DOI: 10.1038/86214

実験手法

SOLUTION NMR