3DVX

Crystal structure of reduced DsbA3 from Neisseria meningitidis

3DVX の概要

• エントリーDOI: 10.2210/pdb3dvx/pdb
• 関連するPDBエントリー: 3DVW
• 分子名称: Thiol:disulfide interchange protein DsbA, SULFATE ION (3 entities in total)
• 機能のキーワード: thiol-oxidoreductase, neisseria, dsba, disulfide bond, oxidoreductase
• 由来する生物種: Neisseria meningitidis MC58
• 細胞内の位置: Periplasm (By similarity): Q9K0Z4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44850.37

構造登録者

Lafaye, C.,Serre, L. (登録日: 2008-07-21, 公開日: 2009-08-04, 最終更新日: 2024-10-16)

主引用文献

Lafaye, C.,Iwema, T.,Carpentier, P.,Jullian-Binard, C.,Kroll, J.S.,Collet, J.F.,Serre, L.
Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis.
J.Mol.Biol., 392:952-966, 2009

PubMed Abstract: Bacterial virulence depends on the correct folding of surface-exposed proteins, a process catalyzed by the thiol-disulfide oxidoreductase DsbA, which facilitates the synthesis of disulfide bonds in Gram-negative bacteria. The Neisseria meningitidis genome possesses three genes encoding active DsbAs: DsbA1, DsbA2 and DsbA3. DsbA1 and DsbA2 have been characterized as lipoproteins involved in natural competence and in host interactive biology, while the function of DsbA3 remains unknown. This work reports the biochemical characterization of the three neisserial enzymes and the crystal structures of DsbA1 and DsbA3. As predicted by sequence homology, both enzymes adopt the classic Escherichia coli DsbA fold. The most striking feature shared by all three proteins is their exceptional oxidizing power. With a redox potential of -80 mV, the neisserial DsbAs are the most oxidizing thioredoxin-like enzymes known to date. Consistent with these findings, thermal studies indicate that their reduced form is also extremely stable. For each of these enzymes, this study shows that a threonine residue found within the active-site region plays a key role in dictating this extraordinary oxidizing power. This result highlights how residues located outside the CXXC motif may influence the redox potential of members of the thioredoxin family.

PubMed: 19631659
DOI: 10.1016/j.jmb.2009.07.056

実験手法

X-RAY DIFFRACTION (2.8 Å)