3HYP

Crystal structure of Bacteroides fragilis TrxP_S105G mutant

3HYP の概要

• エントリーDOI: 10.2210/pdb3hyp/pdb
• 関連するPDBエントリー: 3HXS
• 分子名称: Thioredoxin, ZINC ION (3 entities in total)
• 機能のキーワード: thioredoxin, disulfide bond, electron transport
• 由来する生物種: Bacteroides fragilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32059.46

構造登録者

Shouldice, S.R. (登録日: 2009-06-22, 公開日: 2010-01-12, 最終更新日: 2024-11-13)

主引用文献

Shouldice, S.R.,Cho, S.H.,Boyd, D.,Heras, B.,Eser, M.,Beckwith, J.,Riggs, P.,Martin, J.L.,Berkmen, M.
In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling
Mol.Microbiol., 75:13-28, 2010

PubMed Abstract: Current dogma dictates that bacterial proteins with misoxidized disulfide bonds are shuffled into correctly oxidized states by DsbC. There are two proposed mechanisms for DsbC activity. The first involves a DsbC-only model of substrate disulfide rearrangement. The second invokes cycles of reduction and oxidation of substrate disulfide bonds by DsbC and DsbA respectively. Here, we addressed whether the second mechanism is important in vivo by identifying whether a periplasmic reductase could complement DsbC. We screened for naturally occurring periplasmic reductases in Bacteroides fragilis, a bacterium chosen because we predicted it encodes reductases and has a reducing periplasm. We found that the B. fragilis periplasmic protein TrxP has a thioredoxin fold with an extended N-terminal region; that it is a very active reductase but a poor isomerase; and that it fully complements dsbC. These results provide direct in vivo evidence that correctly folded protein is achievable via cycles of oxidation and reduction.

PubMed: 19968787
DOI: 10.1111/j.1365-2958.2009.06952.x

実験手法

X-RAY DIFFRACTION (2.899 Å)