Subangstrom Resolution X-Ray Structure Details Aquaporin-Water Interactions

Author:

Kosinska Eriksson Urszula1,Fischer Gerhard1,Friemann Rosmarie1,Enkavi Giray2,Tajkhorshid Emad2,Neutze Richard1

Affiliation:

1. Department of Chemistry and Molecular Biology, University of Gothenburg, Box 462, S-40530 Göteborg, Sweden.

2. Department of Biochemistry, College of Medicine, Center for Biophysics and Computational Biology, and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, IL 61802, USA.

Abstract

Choosing Water Aquaporins are proteins that facilitate transport of water across biological membranes. They must be selective for water, without binding it so tightly as to impede transport, and they must prevent proton transfer by rapid exchange between hydrogen-bonded water molecules. Kosinska Eriksson et al. (p. 1346 ; see the Perspective by Abramson and Vartanian ) describe the subangstrom resolution structure of yeast aquaporin, which allows assignment of side-chain conformations and shows that the H-bond geometry of water molecules prevents proton conductance without compromising water transport.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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