3ZOJ
High-resolution structure of Pichia Pastoris aquaporin Aqy1 at 0.88 A
Summary for 3ZOJ
| Entry DOI | 10.2210/pdb3zoj/pdb |
| Descriptor | AQUAPORIN, octyl beta-D-glucopyranoside, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | channel, membrane protein |
| Biological source | KOMAGATAELLA PASTORIS |
| Total number of polymer chains | 1 |
| Total formula weight | 30915.90 |
| Authors | Kosinska-Eriksson, U.,Fischer, G.,Friemann, R.,Enkavi, G.,Tajkhorshid, E.,Neutze, R. (deposition date: 2013-02-21, release date: 2013-06-26, Last modification date: 2023-12-20) |
| Primary citation | Kosinska-Eriksson, U.,Fischer, G.,Friemann, R.,Enkavi, G.,Tajkhorshid, E.,Neutze, R. Subangstrom Resolution X-Ray Structure Details Aquaporin-Water Interactions Science, 340:1346-, 2013 Cited by PubMed Abstract: Aquaporins are membrane channels that facilitate the flow of water across biological membranes. Two conserved regions are central for selective function: the dual asparagine-proline-alanine (NPA) aquaporin signature motif and the aromatic and arginine selectivity filter (SF). Here, we present the crystal structure of a yeast aquaporin at 0.88 angstrom resolution. We visualize the H-bond donor interactions of the NPA motif's asparagine residues to passing water molecules; observe a polarized water-water H-bond configuration within the channel; assign the tautomeric states of the SF histidine and arginine residues; and observe four SF water positions too closely spaced to be simultaneously occupied. Strongly correlated movements break the connectivity of SF waters to other water molecules within the channel and prevent proton transport via a Grotthuss mechanism. PubMed: 23766328DOI: 10.1126/SCIENCE.1234306 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.88 Å) |
Structure validation
Download full validation report
