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

Martin L Williams; David K Chalmers; Jennifer L Martin; Martin J Scanlon

doi:10.1007/s12104-009-9199-8

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

Biomol NMR Assign. 2010 Apr;4(1):25-8. doi: 10.1007/s12104-009-9199-8. Epub 2009 Nov 20.

Authors

Martin L Williams¹, David K Chalmers, Jennifer L Martin, Martin J Scanlon

Affiliation

¹ Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University Parkville Campus, 381 Royal Parade, Parkville, VIC 3052, Australia.

PMID: 19936968
DOI: 10.1007/s12104-009-9199-8

Abstract

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.

MeSH terms

Amino Acid Sequence
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Carbon Isotopes / chemistry
Escherichia coli
Hydrogen / chemistry
Models, Molecular
Nitrogen Isotopes / chemistry
Nuclear Magnetic Resonance, Biomolecular
Oxidation-Reduction
Protein Disulfide Reductase (Glutathione) / chemistry*
Protein Disulfide Reductase (Glutathione) / genetics
Staphylococcus aureus / chemistry*

Substances

Bacterial Proteins
Carbon Isotopes
Nitrogen Isotopes
Hydrogen
Protein Disulfide Reductase (Glutathione)