3PFU

N-terminal domain of Thiol:disulfide interchange protein DsbD in its reduced form

3PFU の概要

• エントリーDOI: 10.2210/pdb3pfu/pdb
• 関連するPDBエントリー: 1JPE 1L6P 1VRS
• 分子名称: Thiol:disulfide interchange protein dsbD, 2,3-DIHYDROXY-1,4-DITHIOBUTANE (3 entities in total)
• 機能のキーワード: immunoglobulin-like fold, thiol disulfide oxidoreductase, periplasmic domain of transmembrane protein, oxidoreductase, electron transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P36655
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15926.93

構造登録者

Mavridou, D.A.I.,Saridakis, E.,Ferguson, S.J.,Redfield, C. (登録日: 2010-10-29, 公開日: 2011-05-04, 最終更新日: 2023-11-01)

主引用文献

Mavridou, D.A.,Saridakis, E.,Kritsiligkou, P.,Goddard, A.D.,Stevens, J.M.,Ferguson, S.J.,Redfield, C.
Oxidation state-dependent protein-protein interactions in disulfide cascades
J.Biol.Chem., 286:24943-24956, 2011

PubMed Abstract: Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms.

PubMed: 21543317
DOI: 10.1074/jbc.M111.236141

実験手法

X-RAY DIFFRACTION (1.8 Å)