Resonance assignments of the metal sensor CzrA in the apo-, Zn2- and DNA-bound (42 kDa) states.
Zn/Co binding to homodimeric CzrA de-represses transcription of the czr (cobalt zinc resistance) operon in Staphylococcus aureus. Essentially complete backbone and stereospecific methyl group resonance assignments for apo-, Zn2 and a 42 kDa apo-CzrA-DNA complex are presented.
Arunkumar
Alphonse I
AI
Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.
Pennella
Mario A
MA
Kong
Xiangming
X
Giedroc
David P
DP
D001059:Apoproteins / Q000737:chemistry / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D004269:DNA, Bacterial / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013211:Staphylococcus aureus / Q000737:chemistry / Q000235:genetics; D015032:Zinc / Q000378:metabolism
D001059:Apoproteins; D001426:Bacterial Proteins; C120278:CzrA protein, Staphylococcus aureus; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D015032:Zinc