title: The architecture of CopA from Archeaoglobus fulgidus studied by cryo-electron microscopy and computational docking.
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.
authors.affiliation: Skirball Institute, New York University School of Medicine, New York, NY 10016, USA.
authors.forename: Gregory S
authors.initials: GS
authors.lastname: Allen
authors.forename: Chen-Chou
authors.initials: CC
authors.lastname: Wu
authors.forename: Tim
authors.initials: T
authors.lastname: Cardozo
authors.forename: David L
authors.initials: DL
authors.lastname: Stokes
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D019611:Archaeoglobus fulgidus / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D003198:Computer Simulation; D020285:Cryoelectron Microscopy; D003460:Crystallization; D003461:Crystallography; D057075:Enzyme Assays; D006868:Hydrolysis; D008958:Models, Molecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; C071263:CopA protein, Bacteria; D000255:Adenosine Triphosphate