1SOR
Aquaporin-0 membrane junctions reveal the structure of a closed water pore
Summary for 1SOR
| Entry DOI | 10.2210/pdb1sor/pdb |
| Descriptor | Aquaporin-0 (1 entity in total) |
| Functional Keywords | membrane junction, water channel, membrane protein |
| Biological source | Ovis aries (sheep) |
| Cellular location | Cell membrane ; Multi- pass membrane protein : Q6J8I9 |
| Total number of polymer chains | 1 |
| Total formula weight | 25173.44 |
| Authors | Gonen, T.,Sliz, P.,Kistler, J.,Cheng, Y.,Walz, T. (deposition date: 2004-03-15, release date: 2004-05-11, Last modification date: 2023-08-23) |
| Primary citation | Gonen, T.,Sliz, P.,Kistler, J.,Cheng, Y.,Walz, T. Aquaporin-0 membrane junctions reveal the structure of a closed water pore Nature, 429:193-197, 2004 Cited by PubMed Abstract: 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. PubMed: 15141214DOI: 10.1038/nature02503 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (3 Å) |
Structure validation
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