Backbone and side chain 1H, 15N and 13C assignments for the oxidised and reduced forms of the oxidoreductase protein DsbA from Staphylococcus aureus.
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.
Williams
Martin L
ML
Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University Parkville Campus, 381 Royal Parade, Parkville, VIC 3052, Australia.
Chalmers
David K
DK
Martin
Jennifer L
JL
Scanlon
Martin J
MJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D002247:Carbon Isotopes / Q000737:chemistry; D004926:Escherichia coli; D006859:Hydrogen / Q000737:chemistry; D008958:Models, Molecular; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D011490:Protein Disulfide Reductase (Glutathione) / Q000737:chemistry* / Q000235:genetics; D013211:Staphylococcus aureus / Q000737:chemistry*
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D006859:Hydrogen; D011490:Protein Disulfide Reductase (Glutathione)