3H93

Crystal Structure of Pseudomonas aeruginosa DsbA

3H93 の概要

• エントリーDOI: 10.2210/pdb3h93/pdb
• 分子名称: Thiol:disulfide interchange protein dsbA, GLYCEROL (3 entities in total)
• 機能のキーワード: disulfide bond, redox-active center, transcription regulator
• 由来する生物種: Pseudomonas aeruginosa PAO1
• 細胞内の位置: Periplasm : P0C2B2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22017.22

構造登録者

Shouldice, S.R. (登録日: 2009-04-29, 公開日: 2009-12-08, 最終更新日: 2024-11-20)

主引用文献

Shouldice, S.R.,Heras, B.,Jarrott, R.,Sharma, P.,Scanlon, M.J.,Martin, J.L.
Characterization of the DsbA Oxidative Folding Catalyst from Pseudomonas aeruginosa Reveals a Highly Oxidizing Protein that Binds Small Molecules.
Antioxid Redox Signal, 12:921-931, 2010

PubMed Abstract: Bacterial antibiotic resistance is an emerging global crisis, and treatment of multidrug-resistant gram-negative infections, particularly those caused by the opportunistic human pathogen Pseudomonas aeruginosa, remains a major challenge. This problem is compounded by a lack of new antibiotics in the development pipeline: only two new classes have been developed since the 1960s, and both are indicated for multidrug-resistant gram-positive infections. A promising new approach to combat antibiotic resistance is by targeting bacterial virulence, rather than bacterial viability. The bacterial periplasmic protein DsbA represents a central point for antivirulence intervention because its oxidoreductase activity is essential for the folding and function of almost all exported virulence factors. Here we describe the three-dimensional structure of this DsbA target from P. aeruginosa, and we establish for the first time that a member of this enzyme family is capable of binding small molecules. We also describe biochemical assays that validate the redox activity of PaDsbA. Together, the structural and functional characterization of PaDsbA provides the basis for future studies aimed at designing a new class of antivirulence compounds to combat antibiotic-resistant P. aeruginosa infection.

PubMed: 19788398
DOI: 10.1089/ars.2009.2736

実験手法

X-RAY DIFFRACTION (1.501 Å)