Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity.
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ABSTRACT:
SUBMITTER: Meloni G
PROVIDER: S-EPMC3947036 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
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Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity.
Meloni Gabriele G Zhang Limei L Rees Douglas C DC
ACS chemical biology 20131101 1
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 ...[more]
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