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

5 Citations (Scopus)

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

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Adenosine Triphosphatases
Metals
Archaeoglobus
X ray absorption
Sulfur
Transition metals
Paramagnetic resonance
Nitrogen
Binding Sites
Electron Spin Resonance Spectroscopy
Ions
Oxygen
Ligands
Membranes
Amino Acids
Geometry
X-Rays

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

Cite this

Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB : Implications for metal selectivity. / Meloni, Gabriele; Zhang, Limei; Rees, Douglas C.

In: ACS Chemical Biology, Vol. 9, No. 1, 17.01.2014, p. 116-121.

Research output: Contribution to journalArticle

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