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：0
作者：
Martin L. Williams
David K. Chalmers
Jennifer L. Martin
Martin J. Scanlon
机构：
[1] Monash University (Parkville Campus),Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences
[2] University of Queensland,Institute for Molecular Bioscience
来源：
Biomolecular NMR Assignments | 2010年 / 4卷
关键词：
Disulfide bond; DsbA; Gram positive;
D O I：
暂无
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学科分类号：
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.
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页码：25 / 28
页数：3
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共 124 条
[1]  
Bax A(1993)Methodological advances in protein NMR Acc Chem Res 26 131-138
[2]  
Grzesiek S(2009)Crystal structure and biophysical properties of J Biol Chem 284 23719-23733
[3]  
Crow A(1995) BdbD An oxidizing thiol:disulfide oxidoreductase containing a novel metal site J Biomol NMR 6 277-293
[4]  
Lewin A(2005)NMRPipe: a multidimensional spectral processing system based on UNIX pipes Arch Microbiol 184 117-118
[5]  
Hecht O(1998) DsbA is a membrane-bound lipoprotein with thiol-disulfide oxidoreductase activity Structure 6 757-767
[6]  
Carlsson Möller M(2007)Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization Acta Crystallogr F 63 953-956
[7]  
Moore GR(2008)Expression and crystallization of DsbA from J Biol Chem 283 4261-4271
[8]  
Hederstedt L(2007) DsbA does not have a destabilizing disulfide Biomol NMR Assign 1 75-76
[9]  
Le Brun NE(2007)Backbone and side-chain J Mol Biol 371 703-716
[10]  
Delaglio F(1997)H, J Mol Biol 268 137-146
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