NMR backbone resonance assignments of the N, P domains of CopA, a copper-transporting ATPase, in the apo and ligand bound states.
Copper-transporting ATPase, a member of P-type ATPase family, plays a key role in the homeostasis of cellular copper levels. Here, the backbone assignments of the directly connected N and P domains (292 residues, 31 kDa) of Cu-transporting ATPase in the ligand free and the AMPPCP-bound states are reported in solution. The NMR assignments pave the way for binding and dynamics studies of this enzyme to better understand its function.
Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, 32306, USA.
Dan
D
Meng
Lei
L
Bruschweiler-Li
Fengli
F
Zhang
Rafael
R
Brüschweiler
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D001059:Apoproteins / Q000737:chemistry* / Q000378:metabolism*; D019611:Archaeoglobus fulgidus / Q000201:enzymology; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000378:metabolism*; D000073840:Copper-Transporting ATPases; D008024:Ligands; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary
D001059:Apoproteins; D027682:Cation Transport Proteins; D008024:Ligands; D000251:Adenosine Triphosphatases; D000073840:Copper-Transporting ATPases