1ORM

NMR FOLD OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES

1ORM の概要

• エントリーDOI: 10.2210/pdb1orm/pdb
• 関連するPDBエントリー: 1QJ8 1QJ9
• 分子名称: Outer membrane protein X (1 entity in total)
• 機能のキーワード: ompx, membrane protein, trosy, dhpc, detergents, lipids, micelles
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P0A917
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16371.77

構造登録者

Fernandez, C.,Adeishvili, K.,Wuthrich, K. (登録日: 2003-03-14, 公開日: 2003-04-22, 最終更新日: 2024-05-22)

主引用文献

FERNANDEZ, C.,ADEISHVILI, K.,WUTHRICH, K.
TRANSVERSE RELAXATION-OPTIMIZED NMR SPECTROSCOPY WITH THE OUTER MEMBRANE PROTEIN OMPX IN DIHEXANOYL PHOSPHATIDYLCHOLINE MICELLES
Proc.Natl.Acad.Sci.USA, 98:2358-2363, 2001

PubMed Abstract: The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX from Escherichia coli was reconstituted with dihexanoyl phosphatidylcholine (DHPC) in mixed micelles of molecular mass of about 60 kDa. Transverse relaxation-optimized spectroscopy (TROSY)-type triple resonance NMR experiments and TROSY-type nuclear Overhauser enhancement spectra were recorded in 2 mM aqueous solutions of these mixed micelles at pH 6.8 and 30 degrees C. Complete sequence-specific NMR assignments for the polypeptide backbone thus have been obtained. The (13)C chemical shifts and the nuclear Overhauser effect data then resulted in the identification of the regular secondary structure elements of OmpX/DHPC in solution and in the collection of an input of conformational constraints for the computation of the global fold of the protein. The same type of polypeptide backbone fold is observed in the presently determined solution structure and the previously reported crystal structure of OmpX determined in the presence of the detergent n-octyltetraoxyethylene. Further structure refinement will have to rely on the additional resonance assignment of partially or fully protonated amino acid side chains, but the present data already demonstrate that relaxation-optimized NMR techniques open novel avenues for studies of structure and function of integral membrane proteins.

PubMed: 11226244
DOI: 10.1073/pnas.051629298

実験手法

SOLUTION NMR