3A3T

The oxidoreductase NmDsbA1 from N. meningitidis

3A3T の概要

• エントリーDOI: 10.2210/pdb3a3t/pdb
• 関連するPDBエントリー: 1DSB 2ZNM
• 分子名称: Thiol:disulfide interchange protein DsbA (2 entities in total)
• 機能のキーワード: thioredoxin-like, dsba fold, oxidoreductase
• 由来する生物種: Neisseria meningitidis serogroup B
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 140954.87

構造登録者

Vivian, J.P.,Scoullar, J.,Bushell, S.,Beddoe, T.,Wilce, M.C.J.,Byres, E.,Boyle, T.P.,Rimmer, K.,Doak, B.,Simpson, J.S.,Graham, B.,Heras, B.,Kahler, C.M.,Rossjohn, J.,Scanlon, M.J. (登録日: 2009-06-19, 公開日: 2009-10-20, 最終更新日: 2024-11-06)

主引用文献

Vivian, J.P.,Scoullar, J.,Rimmer, K.,Bushell, S.R.,Beddoe, T.,Wilce, M.C.J.,Byres, E.,Boyle, T.P.,Doak, B.,Simpson, J.S.,Graham, B.,Heras, B.,Kahler, C.M.,Rossjohn, J.,Scanlon, M.J.
Structure and function of the oxidoreductase DsbA1 from Neisseria meningitidis
J.Mol.Biol., 394:931-943, 2009

PubMed Abstract: Neisseria meningitidis encodes three DsbA oxidoreductases (NmDsbA1-NmDsbA3) that are vital for the oxidative folding of many membrane and secreted proteins, and these three enzymes are considered to exhibit different substrate specificities. This has led to the suggestion that each N. meningitidis DsbA (NmDsbA) may play a specialized role in different stages of pathogenesis; however, the molecular and structural bases of the different roles of NmDsbAs are unclear. With the aim of determining the molecular basis for substrate specificity and how this correlates to pathogenesis, we undertook a biochemical and structural characterization of the three NmDsbAs. We report the 2.0-A-resolution crystal structure of the oxidized form of NmDsbA1, which adopted a canonical DsbA fold similar to that observed in the structures of NmDsbA3 and Escherichia coli DsbA (EcDsbA). Structural comparisons revealed variations around the active site and candidate peptide-binding region. Additionally, we demonstrate that all three NmDsbAs are strong oxidases with similar redox potentials; however, they differ from EcDsbA in their ability to be reoxidized by E. coli DsbB. Collectively, our studies suggest that the small structural differences between the NmDsbA enzymes and EcDsbA are functionally significant and are the likely determinants of substrate specificity.

PubMed: 19815019
DOI: 10.1016/j.jmb.2009.09.065

実験手法

X-RAY DIFFRACTION (2.1 Å)