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Aquaporin-0 membrane junctions reveal the structure of a closed water pore

Author

Listed:
  • Tamir Gonen

    (Harvard Medical School)

  • Piotr Sliz

    (Howard Hughes Medical Institute and Children's Hospital Laboratory of Molecular Medicine
    Harvard Medical School)

  • Joerg Kistler

    (University of Auckland)

  • Yifan Cheng

    (Harvard Medical School)

  • Thomas Walz

    (Harvard Medical School)

Abstract

The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to form membrane junctions in vivo1. We show here that AQP0 from the lens core, containing some carboxy-terminally cleaved AQP02,3, forms double-layered crystals that recapitulate in vivo junctions. We present the structure of the AQP0 membrane junction as determined by electron crystallography. The junction is formed by three localized interactions between AQP0 molecules in adjoining membranes, mainly mediated by proline residues conserved in AQP0s from different species but not present in most other aquaporins. Whereas all previously determined aquaporin structures show the pore in an open conformation4,5,6,7,8,9, the water pore is closed in AQP0 junctions. The water pathway in AQP0 also contains an additional pore constriction, not seen in other known aquaporin structures4,5,6,7,8,9, which may be responsible for pore gating.

Suggested Citation

  • Tamir Gonen & Piotr Sliz & Joerg Kistler & Yifan Cheng & Thomas Walz, 2004. "Aquaporin-0 membrane junctions reveal the structure of a closed water pore," Nature, Nature, vol. 429(6988), pages 193-197, May.
    • Handle: RePEc:nat:nature:v:429:y:2004:i:6988:d:10.1038_nature02503
    DOI: 10.1038/nature02503
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