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

页码：25 / 28

页数：4

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