Structure of a copper pump suggests a regulatory role for its metal-binding domain

Structure. 2008 Jun;16(6):976-85. doi: 10.1016/j.str.2008.02.025.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Archaeal Proteins / chemistry*
  • Archaeoglobus fulgidus
  • Cation Transport Proteins / chemistry*
  • Copper / chemistry*
  • Copper-Transporting ATPases
  • Cryoelectron Microscopy
  • Crystallization
  • Image Processing, Computer-Assisted
  • Models, Molecular*
  • Protein Structure, Tertiary


  • Archaeal Proteins
  • Cation Transport Proteins
  • Copper
  • Adenosine Triphosphatases
  • Copper-Transporting ATPases

Associated data

  • PDB/2VOY