Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: Implications for metal selectivity

Gabriele Meloni, Limei Zhang, Douglas C. Rees

Research output: Contribution to journalArticle

6 Scopus citations

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 f ulgidus 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 Cu2+ center in which a single cupric ion is coordinated in a distorted square pyramidal geometry by mixed nitrogen/oxygen and sulfur ligands.

Original languageEnglish (US)
Pages (from-to)116-121
Number of pages6
JournalACS chemical biology
Volume9
Issue number1
DOIs
StatePublished - Jan 17 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

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