2W2E
1.15 Angstrom crystal structure of P.pastoris aquaporin, Aqy1, in a closed conformation at pH 3.5
Summary for 2W2E
| Entry DOI | 10.2210/pdb2w2e/pdb |
| Related | 2W1P |
| Descriptor | AQUAPORIN PIP2-7 7, octyl beta-D-glucopyranoside, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | yeast, gating, membrane protein |
| Biological source | KOMAGATAELLA PASTORIS |
| Total number of polymer chains | 1 |
| Total formula weight | 31793.01 |
| Authors | Fischer, G.,Kosinska-Eriksson, U.,Aponte-Santamaria, C.,Palmgren, M.,Geijer, C.,Hedfalk, K.,Hohmann, S.,de Groot, B.L.,Neutze, R.,Lindkvist-Petersson, K. (deposition date: 2008-10-29, release date: 2009-06-16, Last modification date: 2023-12-13) |
| Primary citation | Fischer, G.,Kosinska-Eriksson, U.,Aponte-Santamaria, C.,Palmgren, M.,Geijer, C.,Hedfalk, K.,Hohmann, S.,De Groot, B.L.,Neutze, R.,Lindkvist-Petersson, K. Crystal Structure of a Yeast Aquaporin at 1.15 A Reveals a Novel Gating Mechanism.1.15 A Plos Biol., 7:E130-, 2009 Cited by PubMed Abstract: Aquaporins are transmembrane proteins that facilitate the flow of water through cellular membranes. An unusual characteristic of yeast aquaporins is that they frequently contain an extended N terminus of unknown function. Here we present the X-ray structure of the yeast aquaporin Aqy1 from Pichia pastoris at 1.15 A resolution. Our crystal structure reveals that the water channel is closed by the N terminus, which arranges as a tightly wound helical bundle, with Tyr31 forming H-bond interactions to a water molecule within the pore and thereby occluding the channel entrance. Nevertheless, functional assays show that Aqy1 has appreciable water transport activity that aids survival during rapid freezing of P. pastoris. These findings establish that Aqy1 is a gated water channel. Mutational studies in combination with molecular dynamics simulations imply that gating may be regulated by a combination of phosphorylation and mechanosensitivity. PubMed: 19529756DOI: 10.1371/JOURNAL.PBIO.1000130 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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