Structural determinants of water permeation through aquaporin-1

Kazuyoshi Murata, Kaoru Mitsuoka, Teruhisa Hirai, Thomas Walz, Peter Agre, J. Bernard Heymann, Andreas Engel and Yoshinori Fujiyoshi ()
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Kazuyoshi Murata: National Institute for Physiological Sciences
Kaoru Mitsuoka: Faculty of Science, Kyoto University
Teruhisa Hirai: Faculty of Science, Kyoto University
Thomas Walz: Harvard Medical School
Peter Agre: Johns Hopkins University School of Medicine
J. Bernard Heymann: M. E. Müller-Institute for Microscopy at the Biozentrum, University of Basel
Andreas Engel: M. E. Müller-Institute for Microscopy at the Biozentrum, University of Basel
Yoshinori Fujiyoshi: Faculty of Science, Kyoto University

Nature, 2000, vol. 407, issue 6804, 599-605

Abstract: 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 3.8 Å 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 Å 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.

Date: 2000
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DOI: 10.1038/35036519

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