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Structural basis for alternating access of a eukaryotic calcium/proton exchanger

Author

Listed:
  • Andrew B. Waight

    (University of California)

  • Bjørn Panyella Pedersen

    (University of California)

  • Avner Schlessinger

    (California Institute for Quantitative Biosciences, University of California)

  • Massimiliano Bonomi

    (California Institute for Quantitative Biosciences, University of California)

  • Bryant H. Chau

    (University of California)

  • Zygy Roe-Zurz

    (University of California)

  • Aaron J. Risenmay

    (University of California)

  • Andrej Sali

    (California Institute for Quantitative Biosciences, University of California)

  • Robert M. Stroud

    (University of California)

Abstract

The X-ray crystal structure of a member of the Ca2+/H+ (CAX) antiporter family from Saccharomyces cerevisiae in a cytosol-facing, substrate-bound conformation is solved; using the structure, a mechanism by which members of the Ca2+:cation (CaCA) superfamily facilitate Ca2+ transport across cellular membranes is proposed.

Suggested Citation

  • Andrew B. Waight & Bjørn Panyella Pedersen & Avner Schlessinger & Massimiliano Bonomi & Bryant H. Chau & Zygy Roe-Zurz & Aaron J. Risenmay & Andrej Sali & Robert M. Stroud, 2013. "Structural basis for alternating access of a eukaryotic calcium/proton exchanger," Nature, Nature, vol. 499(7456), pages 107-110, July.
    • Handle: RePEc:nat:nature:v:499:y:2013:i:7456:d:10.1038_nature12233
    DOI: 10.1038/nature12233
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