7PQF

Crystal structure of Campylobacter jejuni DsbA2

7PQF の概要

• エントリーDOI: 10.2210/pdb7pqf/pdb
• 関連するPDBエントリー: 7PQ7 7PQ8
• 分子名称: Thiol:disulfide interchange protein DsbA/DsbL (2 entities in total)
• 機能のキーワード: periplasmic, disulfide bond, thioredoxin fold, posttranslational modification, oxidoreductase
• 由来する生物種: Campylobacter jejuni
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23385.68

構造登録者

Wilk, P.,Banas, A.M.,Bocian-Ostrzycka, K.M.,Jagusztyn-Krynicka, E.K. (登録日: 2021-09-17, 公開日: 2021-12-29, 最終更新日: 2024-11-20)

主引用文献

Banas, A.M.,Bocian-Ostrzycka, K.M.,Dunin-Horkawicz, S.,Ludwiczak, J.,Wilk, P.,Orlikowska, M.,Wyszynska, A.,Dabrowska, M.,Plichta, M.,Spodzieja, M.,Polanska, M.A.,Malinowska, A.,Jagusztyn-Krynicka, E.K.
Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of Campylobacter jejuni and Their Impact on Bacterial Physiology and Pathogenesis.
Int J Mol Sci, 22:-, 2021

PubMed Abstract: The bacterial proteins of the Dsb family catalyze the formation of disulfide bridges between cysteine residues that stabilize protein structures and ensure their proper functioning. Here, we report the detailed analysis of the Dsb pathway of . The oxidizing Dsb system of this pathogen is unique because it consists of two monomeric DsbAs (DsbA1 and DsbA2) and one dimeric bifunctional protein (C8J_1298). Previously, we showed that DsbA1 and C8J_1298 are redundant. Here, we unraveled the interaction between the two monomeric DsbAs by in vitro and in vivo experiments and by solving their structures and found that both monomeric DsbAs are dispensable proteins. Their structures confirmed that they are homologs of EcDsbL. The slight differences seen in the surface charge of the proteins do not affect the interaction with their redox partner. Comparative proteomics showed that several respiratory proteins, as well as periplasmic transport proteins, are targets of the Dsb system. Some of these, both donors and electron acceptors, are essential elements of the respiratory process under oxygen-limiting conditions in the host intestine. The data presented provide detailed information on the function of the Dsb system, identifying it as a potential target for novel antibacterial molecules.

PubMed: 34948248
DOI: 10.3390/ijms222413451

実験手法

X-RAY DIFFRACTION (1.82 Å)