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PDBsum entry 1sor

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Membrane protein PDB id
1sor
Contents
Protein chain
235 a.a. *
* Residue conservation analysis

References listed in PDB file
Key reference
Title Aquaporin-0 membrane junctions reveal the structure of a closed water pore.
Authors T.Gonen, P.Sliz, J.Kistler, Y.Cheng, T.Walz.
Ref. Nature, 2004, 429, 193-197. [DOI no: 10.1038/nature02503]
PubMed id 15141214
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.
Figure 2.
Figure 2: The AQP0-mediated membrane junction. a, Ribbon representation of the membrane junction with the positions of the two membranes indicated in yellow. b, The Pro 38 residues contributed by all eight AQP0 subunits in the two interacting tetramers. c, Corresponding area of the 2F[o] -F[c]map. d, The C loops connect each AQP0 molecule to two molecules in the opposite membrane. Letters A to D refer to the molecules described in the text. e, Corresponding area of the 2F[o] -F[c] map. Panels a, b and d were created with Chimera^29 and panels c and e with the program O28.
Figure 3.
Figure 3: The closed AQP0 water pore. a, b, Side chains lining the pores in AQP1 (a) and AQP0 (b). c, The left panel shows pore profiles for AQP0 (red) and AQP1 (green) generated with the program 'HOLE'. The positions of the NPA motifs, the ar/R constriction site in AQP1 and the two constriction sites in AQP0 (CS-I, CS-II) are marked and shown in red. The pore profiles are aligned with the models of AQP1 (middle panel) and AQP0 (right panel). Panels a and b were created with Chimera^29.
The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2004, 429, 193-197) copyright 2004.
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