Identification of the site of [alpha-32P]ATP adduct formation in the ArsA protein.
The ArsA protein, the catalytic subunit of the oxyanion-translocating ATPase encoded by the bacterial plasmid-encoded ars operon, and truncated derivatives were labeled with alpha-[32P]ATP. The labeled polypeptides were cleaved with cyanogen bromide. From gas-phase microsequencing the site of labeling was deduced to lie within residues 283-323 of the ArsA protein, a region postulated to be in a flexible linker connecting the two homologous halves of the ArsA protein.
Kaur
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Department of Biochemistry, School of Medicine, Wayne State University, Detroit, Michigan 48201.
Rosen
B P
BP
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000737:chemistry*; D000595:Amino Acid Sequence; D053501:Arsenite Transporting ATPases; D001665:Binding Sites; D003488:Cyanogen Bromide; D006868:Hydrolysis; D016623:Ion Pumps; D008027:Light; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes; D010084:Oxidation-Reduction; D010761:Phosphorus Radioisotopes; D012697:Serine Endopeptidases
D016623:Ion Pumps; D008565:Membrane Proteins; D009097:Multienzyme Complexes; D010761:Phosphorus Radioisotopes; D000255:Adenosine Triphosphate; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D000251:Adenosine Triphosphatases; D053501:Arsenite Transporting ATPases; D003488:Cyanogen Bromide