1A2L

REDUCED DSBA AT 2.7 ANGSTROMS RESOLUTION

1A2L の概要

• エントリーDOI: 10.2210/pdb1a2l/pdb
• 分子名称: DISULFIDE BOND FORMATION PROTEIN (2 entities in total)
• 機能のキーワード: oxidoreductase, protein disulfide isomerase, protein folding, redox protein, redox-active center
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42310.05

構造登録者

Martin, J.L.,Guddat, L.W. (登録日: 1998-01-06, 公開日: 1998-07-08, 最終更新日: 2024-05-22)

主引用文献

Guddat, L.W.,Bardwell, J.C.,Martin, J.L.
Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization.
Structure, 6:757-767, 1998

PubMed Abstract: The redox proteins that incorporate a thioredoxin fold have diverse properties and functions. The bacterial protein-folding factor DsbA is the most oxidizing of the thioredoxin family. DsbA catalyzes disulfide-bond formation during the folding of secreted proteins. The extremely oxidizing nature of DsbA has been proposed to result from either domain motion or stabilizing active-site interactions in the reduced form. In the domain motion model, hinge bending between the two domains of DsbA occurs as a result of redox-related conformational changes.

PubMed: 9655827
DOI: 10.1016/S0969-2126(98)00077-X

実験手法

X-RAY DIFFRACTION (2.7 Å)