4K2D

Crystal structure of Burkholderia Pseudomallei DsbA

4K2D の概要

• エントリーDOI: 10.2210/pdb4k2d/pdb
• 分子名称: Thiol:disulfide interchange protein, GLYCEROL (3 entities in total)
• 機能のキーワード: thioredoxin fold, disulfide oxidoreductase, oxidoreductase
• 由来する生物種: Burkholderia pseudomallei
• 細胞内の位置: Periplasm (By similarity): Q63Y08
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22298.40

構造登録者

McMahon, R.M. (登録日: 2013-04-09, 公開日: 2013-08-14, 最終更新日: 2024-10-30)

主引用文献

Ireland, P.M.,McMahon, R.M.,Marshall, L.E.,Halili, M.,Furlong, E.,Tay, S.,Martin, J.L.,Sarkar-Tyson, M.
Disarming Burkholderia pseudomallei: Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In Vivo.
Antioxid Redox Signal, 20:606-617, 2014

PubMed Abstract: The intracellular pathogen Burkholderia pseudomallei causes the disease melioidosis, a major source of morbidity and mortality in southeast Asia and northern Australia. The need to develop novel antimicrobials is compounded by the absence of a licensed vaccine and the bacterium's resistance to multiple antibiotics. In a number of clinically relevant Gram-negative pathogens, DsbA is the primary disulfide oxidoreductase responsible for catalyzing the formation of disulfide bonds in secreted and membrane-associated proteins. In this study, a putative B. pseudomallei dsbA gene was evaluated functionally and structurally and its contribution to infection assessed.

PubMed: 23901809
DOI: 10.1089/ars.2013.5375

実験手法

X-RAY DIFFRACTION (1.9 Å)