The Architecture of CopA From Archeaoglobus Fulgidus Studied by Cryo-Electron Microscopy and Computational Docking

Structure. 2011 Sep 7;19(9):1219-32. doi: 10.1016/j.str.2011.05.014. Epub 2011 Aug 4.

Abstract

CopA uses ATP to pump Cu(+) across cell membranes. X-ray crystallography has defined atomic structures of several related P-type ATPases. We have determined a structure of CopA at 10 Å resolution by cryo-electron microscopy of a new crystal form and used computational molecular docking to study the interactions between the N-terminal metal-binding domain (NMBD) and other elements of the molecule. We found that the shorter-chain lipids used to produce these crystals are associated with movements of the cytoplasmic domains, with a novel dimer interface and with disordering of the NMBD, thus offering evidence for the transience of its interaction with the other cytoplasmic domains. Docking identified a binding site that matched the location of the NMBD in our previous structure by cryo-electron microscopy, allowing a more detailed view of its binding configuration and further support for its role in autoinhibition.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Archaeoglobus fulgidus / enzymology*
  • Bacterial Proteins / chemistry*
  • Computer Simulation
  • Cryoelectron Microscopy*
  • Crystallization
  • Crystallography
  • Enzyme Assays
  • Hydrolysis
  • Models, Molecular
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary

Substances

  • Bacterial Proteins
  • CopA protein, Bacteria
  • Adenosine Triphosphate

Associated data

  • PDB/3J08
  • PDB/3J09