Transmembrane Type-2-like Cu^(2+) Site in the P_(1B-3)-type ATPase CopB: Implications for Metal Selectivity
- Creators
- Meloni, Gabriele
- Zhang, Limei
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Rees, Douglas C.
Abstract
Metal selectivity in P_(1B)-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 P_(1B-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.
Additional Information
© 2013 American Chemical Society. Received: August 12, 2013; accepted: October 21, 2013; published: October 21, 2013. The work was supported by National Institutes of Health (NIH) (grant No. GM45162 to D.C.R.), by a Swiss National Science Foundation fellowship for prospective researchers (to G.M.), by a Marie Curie International Outgoing Fellowship (European Commission, grant No. 252961 to G.M.), and by a NSERC PDF award (to L.Z.). We thank Poul Nissen (University of Aarhus, Denmark) for supervising the Marie Curie Fellowship. We thank the staff at Beamline 7-3, Stanford Synchrotron Radiation Lightsource (SSRL), and staff at HXMA Beamline, Canadian Light Source (CLS). SSRL is operated for the DOE and supported by OBER and by the NIH, NIGMS (P41GM103393), and the NCRR (P41RR001209). CLS is supported by NSERC, NRC, CIHR, and the University of Saskatchewan. We thank O. Lewinson and A. T. Lee for providing the full-length cDNA of CopB and A. Di Bilio for assistance with EPR measurements. This project benefited from discussion with Nathan Dalleska and instrumentation made available by the Caltech Environmental Analysis Center.Attached Files
Accepted Version - nihms537544.pdf
Supplemental Material - cb400603t_si_001.pdf
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Additional details
- PMCID
- PMC3947036
- Eprint ID
- 44074
- Resolver ID
- CaltechAUTHORS:20140228-145854857
- NIH
- GM45162
- Swiss National Science Foundation (SNSF)
- Marie Curie Fellowship
- 252961
- OBER
- NIH
- P41GM103393
- NIH
- P41RR001209
- Natural Sciences and Engineering Research Council of Canada (NSERC)
- National Research Council of Canada
- Canadian Institutes of Health Research (CIHR)
- University of Saskatchewan
- Created
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2014-03-01Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field