P-type ATPases play an important role in Cu homeostasis, which provides sufficient Cu for metalloenzyme biosynthesis but prevents oxidative damage of free Cu to the cell. The P(IB) group of P-type ...P-type ATPases play an important role in Cu homeostasis, which provides sufficient Cu for metalloenzyme biosynthesis but prevents oxidative damage of free Cu to the cell. The P(IB) group of P-type ATPases includes ATP-dependent pumps of Cu and other transition metal ions, and it is distinguished from other family members by the presence of N-terminal metal-binding domains (MBD). We have determined structures of two constructs of a Cu pump from Archaeoglobus fulgidus (CopA) by cryoelectron microscopy of tubular crystals, which reveal the overall architecture and domain organization of the molecule. By comparing these structures, we localized its N-terminal MBD within the cytoplasmic domains that use ATP hydrolysis to drive the transport cycle. We have built a pseudoatomic model by fitting existing crystallographic structures into the cryoelectron microscopy maps for CopA, which suggest a Cu-dependent regulatory role for the MBD.
EMDB-5004: Structure of the Copper Transporting ATPase of A. fulgidus by Cryo-electron microscopy. PDB-2voy: CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus Method: EM (helical sym.) / Resolution: 17.5 Å
EMDB-5005: Structure of the Copper Transporting ATPase of A. fulgidus by Cryo-electron microscopy. PDB-2voy: CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus Method: EM (helical sym.) / Resolution: 17.5 Å
Source
bacillus subtilis (bacteria)
archaeoglobus fulgidus (archaea)
oryctolagus cuniculus (rabbit)
Keywords
HYDROLASE / HYDROLASEP-TYPE ATPASE / CRYO-EM / HELICAL RECONSTRUCTION / MEMBRANE PROTEIN / COPPER TRANSPORTER / METAL BINDING DOMAIN
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HYDROLASE / HYDROLASEP-TYPE ATPASE / 
