Backbone and side chain 1H, 15N and 13C assignments for the oxidised and reduced forms of the oxidoreductase protein DsbA from Staphylococcus aureus

被引：2
|
作者：
Williams, Martin L. [1 ]
Chalmers, David K. [1 ]
Martin, Jennifer L. [2 ]
Scanlon, Martin J. [1 ]
机构：
[1] Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
[2] Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2010年 / 4卷 / 01期
关键词：
Oxidoreductase; Disulfide bond; DsbA; Staphylococcus aureus; Gram positive; DISULFIDE BOND FORMATION; VIBRIO-CHOLERAE; BIOCHEMICAL-CHARACTERIZATION; DESTABILIZING DISULFIDE; CRYSTAL-STRUCTURE; NMR;
D O I：
10.1007/s12104-009-9199-8
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
The function and dynamics of the thiol-disulfide oxidoreductase DsbA in the low-GC gram positive bacterium, Staphylococcus aureus, are yet to be elucidated. Here we report 13C, 15N and 1H assignments for the oxidised and reduced forms of SaDsbA as a prelude to further studies on the enzyme.
引用
收藏
页码：25 / 28
页数：4
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