2LTQ

High resolution structure of DsbB C41S by joint calculation with solid-state NMR and X-ray data

2LTQ の概要

• エントリーDOI: 10.2210/pdb2ltq/pdb
• 関連するPDBエントリー: 2LEG 2ZUQ
• NMR情報: BMRB: 18493
• 分子名称: Disulfide bond formation protein B, Fab fragment light chain, Fab fragment heavy chain, ... (4 entities in total)
• 機能のキーワード: membrane protein, oxidoreductase, disulfide bond, redox-active center, cell inner membrane, cell membrane, chaperone, electron transport, membrane, transmembrane, transport
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0A6M2
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 141729.91

構造登録者

Tang, M.,Sperling, L.J.,Schwieters, C.D.,Nesbitt, A.E.,Gennis, R.B.,Rienstra, C.M. (登録日: 2012-05-30, 公開日: 2013-02-27, 最終更新日: 2024-11-27)

主引用文献

Tang, M.,Nesbitt, A.E.,Sperling, L.J.,Berthold, D.A.,Schwieters, C.D.,Gennis, R.B.,Rienstra, C.M.
Structure of the Disulfide Bond Generating Membrane Protein DsbB in the Lipid Bilayer.
J.Mol.Biol., 425:1670-1682, 2013

PubMed Abstract: The integral membrane protein DsbB in Escherichia coli is responsible for oxidizing the periplasmic protein DsbA, which forms disulfide bonds in substrate proteins. We have developed a high-resolution structural model by combining experimental X-ray and solid-state NMR with molecular dynamics (MD) simulations. We embedded the high-resolution DsbB structure, derived from the joint calculation with X-ray reflections and solid-state NMR restraints, into the lipid bilayer and performed MD simulations to provide a mechanistic view of DsbB function in the membrane. Further, we revealed the membrane topology of DsbB by selective proton spin diffusion experiments, which directly probe the correlations of DsbB with water and lipid acyl chains. NMR data also support the model of a flexible periplasmic loop and an interhelical hydrogen bond between Glu26 and Tyr153.

PubMed: 23416557
DOI: 10.1016/j.jmb.2013.02.009

実験手法

SOLID-STATE NMR