title: Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity.
abstract: Metal selectivity in P1B-type ATPase transporters is determined by conserved amino acid residues in their transmembrane helices responsible for metal binding and transport across the cellular membrane. The Cu(2+)-selective CopB from Archaeoglobus fulgidus has been investigated to explore the coordination chemistry of the transition metal binding sites in P1B-3-type ATPases. Electronic absorption, electron paramagnetic resonance, and X-ray absorption spectroscopic studies indicate the presence of a high-affinity transmembrane Type-2-like Cu(2+) center in which a single cupric ion is coordinated in a distorted square pyramidal geometry by mixed nitrogen/oxygen and sulfur ligands.
authors.affiliation: Division of Chemistry and Chemical Engineering and ‡Howard Hughes Medical Institute, California Institute of Technology , Pasadena, California 91125, United States of America.
authors.forename: Gabriele
authors.initials: G
authors.lastname: Meloni
authors.forename: Limei
authors.initials: L
authors.lastname: Zhang
authors.forename: Douglas C
authors.initials: DC
authors.lastname: Rees
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D019611:Archaeoglobus fulgidus / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D001665:Binding Sites; D027682:Cation Transport Proteins / Q000737:chemistry* / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D000079922:Copper Transport Proteins; D004578:Electron Spin Resonance Spectroscopy; D008670:Metals / Q000378:metabolism; D011487:Protein Conformation; D056928:X-Ray Absorption Spectroscopy
chemical_list: D019843:Archaeal Proteins; D027682:Cation Transport Proteins; C489503:CopB protein, Archaea; D000079922:Copper Transport Proteins; D008670:Metals; D003300:Copper; D000251:Adenosine Triphosphatases