1ymg | pdb_00001ymg

The Channel Architecture of Aquaporin O at 2.2 Angstrom Resolution

spinqualitylabelsall models 1ymg, resolution 2.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ymg is a 1 chain structure with sequence from Bos taurus. This structure supersedes the now removed PDB entry 1tm8. The May 2014 RCSB PDB Molecule of the Month feature on Aquaporin by David Goodsell is 10.2210/rcsb_pdb/mom_2014_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BNG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MIP_BOVIN] Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We determined the x-ray structure of bovine aquaporin 0 (AQP0) to a resolution of 2.2 A. The structure of this eukaryotic, integral membrane protein suggests that the selectivity of AQP0 for water transport is based on the identity and location of signature amino acid residues that are hallmarks of the water-selective arm of the AQP family of proteins. Furthermore, the channel lumen is narrowed only by two, quasi-2-fold related tyrosine side chains that might account for reduced water conductance relative to other AQPs. The channel is functionally open to the passage of water because there are eight discreet water molecules within the channel. Comparison of this structure with the recent electron-diffraction structure of the junctional form of sheep AQP0 at pH 6.0 that was interpreted as closed shows no global change in the structure of AQP0 and only small changes in side-chain positions. We observed no structural change to the channel or the molecule as a whole at pH 10, which could be interpreted as the postulated pH-gating mechanism of AQP0-mediated water transport at pH >6.5. Contrary to the electron-diffraction structure, the comparison shows no evidence of channel gating induced by association of the extracellular domains of AQP0 at pH 6.0. Our structure aids the analysis of the interaction of the extracellular domains and the possibility of a cell-cell adhesion role for AQP0. In addition, our structure illustrates the basis for formation of certain types of cataracts that are the result of mutations. The channel architecture of aquaporin 0 at a 2.2-A resolution.,Harries WE, Akhavan D, Miercke LJ, Khademi S, Stroud RM Proc Natl Acad Sci U S A. 2004 Sep 28;101(39):14045-50. Epub 2004 Sep 17. PMID:15377788 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aquaporin

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