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 手法: EM (らせん対称) / 解像度: 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 手法: EM (らせん対称) / 解像度: 17.5 Å