1FQY
STRUCTURE OF AQUAPORIN-1 AT 3.8 A RESOLUTION BY ELECTRON CRYSTALLOGRAPHY
Summary for 1FQY
| Entry DOI | 10.2210/pdb1fqy/pdb |
| Descriptor | AQUAPORIN-1 (1 entity in total) |
| Functional Keywords | water channel, two-dimensional crystal, membrane protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane ; Multi-pass membrane protein : P29972 |
| Total number of polymer chains | 1 |
| Total formula weight | 28549.91 |
| Authors | Murata, K.,Mitsuoka, K.,Hirai, T.,Walz, T.,Agre, P.,Heymann, J.B.,Engel, A.,Fujiyoshi, Y. (deposition date: 2000-09-07, release date: 2000-10-18, Last modification date: 2024-04-17) |
| Primary citation | Murata, K.,Mitsuoka, K.,Hirai, T.,Walz, T.,Agre, P.,Heymann, J.B.,Engel, A.,Fujiyoshi, Y. Structural determinants of water permeation through aquaporin-1. Nature, 407:599-605, 2000 Cited by PubMed Abstract: Human red cell AQP1 is the first functionally defined member of the aquaporin family of membrane water channels. Here we describe an atomic model of AQP1 at 3.8A resolution from electron crystallographic data. Multiple highly conserved amino-acid residues stabilize the novel fold of AQP1. The aqueous pathway is lined with conserved hydrophobic residues that permit rapid water transport, whereas the water selectivity is due to a constriction of the pore diameter to about 3 A over a span of one residue. The atomic model provides a possible molecular explanation to a longstanding puzzle in physiology-how membranes can be freely permeable to water but impermeable to protons. PubMed: 11034202DOI: 10.1038/35036519 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (3.8 Å) |
Structure validation
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