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TitleAquaporin-0 membrane junctions reveal the structure of a closed water pore.
Journal, issue, pagesNature, Vol. 429, Issue 6988, Page 193-197, Year 2004
Publish dateMay 13, 2004
AuthorsTamir Gonen / Piotr Sliz / Joerg Kistler / Yifan Cheng / Thomas Walz /
PubMed AbstractThe lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to form membrane junctions in vivo. We show here that AQP0 from the lens core, containing some carboxy-terminally cleaved ...The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to form membrane junctions in vivo. We show here that AQP0 from the lens core, containing some carboxy-terminally cleaved AQP0, 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 conformation, 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 structures, which may be responsible for pore gating.
External linksNature / PubMed:15141214
MethodsEM (electron crystallography)
Resolution3 Å
Structure data

PDB-1sor:
Aquaporin-0 membrane junctions reveal the structure of a closed water pore
Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 3.0 Å

Source
  • ovis aries (sheep)
KeywordsMEMBRANE PROTEIN / membrane junction / water channel

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