2MNH

Refined structure of outer membrane protein x in nanodisc by measuring residual dipolar couplings

2MNH の概要

• エントリーDOI: 10.2210/pdb2mnh/pdb
• NMR情報: BMRB: 19892
• 分子名称: Outer membrane protein X (1 entity in total)
• 機能のキーワード: beta barrel, membrane protein, residual dipolar coupling, nanodisc, ompx
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16371.77

構造登録者

Bibow, S.,Carneiro, M.G.,Sabo, T.M.,Schwiegk, C.,Becker, S.,Riek, R.,Lee, D. (登録日: 2014-04-05, 公開日: 2015-03-18, 最終更新日: 2024-05-01)

主引用文献

Bibow, S.,Carneiro, M.G.,Sabo, T.M.,Schwiegk, C.,Becker, S.,Riek, R.,Lee, D.
Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.
Protein Sci., 23:851-856, 2014

PubMed Abstract: Membrane proteins are involved in numerous vital biological processes. To understand membrane protein functionality, accurate structural information is required. Usually, structure determination and dynamics of membrane proteins are studied in micelles using either solution state NMR or X-ray crystallography. Even though invaluable information has been obtained by this approach, micelles are known to be far from ideal mimics of biological membranes often causing the loss or decrease of membrane protein activity. Recently, nanodiscs, which are composed of a lipid bilayer surrounded by apolipoproteins, have been introduced as a more physiological alternative than micelles for NMR investigations on membrane proteins. Here, we show that membrane protein bond orientations in nanodiscs can be obtained by measuring residual dipolar couplings (RDCs) with the outer membrane protein OmpX embedded in nanodiscs using Pf1 phage as an alignment medium. The presented collection of membrane protein RDCs in nanodiscs represents an important step toward more comprehensive structural and dynamical NMR-based investigations of membrane proteins in a natural bilayer environment.

PubMed: 24752984
DOI: 10.1002/pro.2482

実験手法

SOLUTION NMR