2ZZ9
Structure of aquaporin-4 S180D mutant at 2.8 A resolution by electron crystallography
Summary for 2ZZ9
| Entry DOI | 10.2210/pdb2zz9/pdb |
| Related | 2D57 |
| Descriptor | Aquaporin-4, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (3 entities in total) |
| Functional Keywords | water transport, water channel, aquaporin, two-dimensional crystal, membrane protein, baculovirus expression system, glycoprotein, membrane, phosphoprotein, transmembrane, transport, transport protein |
| Biological source | Rattus norvegicus (Rat) |
| Cellular location | Membrane; Multi-pass membrane protein: P47863 |
| Total number of polymer chains | 1 |
| Total formula weight | 35937.56 |
| Authors | Tani, K.,Mitsuma, T.,Hiroaki, Y.,Kamegawa, A.,Nishikawa, K.,Tanimura, Y.,Fujiyoshi, Y. (deposition date: 2009-02-06, release date: 2009-06-09, Last modification date: 2023-11-08) |
| Primary citation | Tani, K.,Mitsuma, T.,Hiroaki, Y.,Kamegawa, A.,Nishikawa, K.,Tanimura, Y.,Fujiyoshi, Y. Mechanism of Aquaporin-4's Fast and Highly Selective Water Conduction and Proton Exclusion. J.Mol.Biol., 389:694-706, 2009 Cited by PubMed Abstract: Members of the aquaporin (AQP) family are expressed in almost every organism, including 13 homologues in humans. Based on the electron crystallographic structure of AQP1, the hydrogen-bond isolation mechanism was proposed to explain why AQPs are impermeable to protons despite their very fast water conduction. The mechanism by which AQPs exclude protons remained controversial, however. Here we present the structure of AQP4 at 2.8 A resolution obtained by electron crystallography of double-layered two-dimensional crystals. The resolution has been improved from the previous 3.2 A, with accompanying improvement in data quality resulting in the ability to identify individual water molecules. Our structure of AQP4, the predominant water channel in the brain, reveals eight water molecules in the channel. The arrangement of the waters provides support for the hydrogen-bond isolation mechanism. Our AQP4 structure also visualizes five lipids, showing that direct interactions of the extracellular surface of AQP4 with three lipids in the adjoining membrane help stabilize the membrane junction. PubMed: 19406128DOI: 10.1016/j.jmb.2009.04.049 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (2.8 Å) |
Structure validation
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