Journal
SCIENCE
Volume 340, Issue 6138, Pages 1346-1349Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1234306
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Funding
- European Union Integrated Project EDICT
- Marie Curie Training Network Aqua(glycero)porins
- Olle Engkvist Foundation
- Swedish Research Council
- NIH [R01-GM086749, U54-GM087519, P41-GM104601]
- NSF supercomputing centers [MCA06N060]
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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.
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