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Science 20 October 2000:
Vol. 290. no. 5491, pp. 481 - 486
DOI: 10.1126/science.290.5491.481
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Research Articles

Structure of a Glycerol-Conducting Channel and the Basis for Its Selectivity

Daxiong Fu, Andrew Libson, Larry J. W. Miercke, Cindy Weitzman, Peter Nollert, Jolanta Krucinski, Robert M. Stroud*

Membrane channel proteins of the aquaporin family are highly selective for permeation of specific small molecules, with absolute exclusion of ions and charged solutes and without dissipation of the electrochemical potential across the cell membrane. We report the crystal structure of the Escherichia coli glycerol facilitator (GlpF) with its primary permeant substrate glycerol at 2.2 angstrom resolution. Glycerol molecules line up in an amphipathic channel in single file. In the narrow selectivity filter of the channel the glycerol alkyl backbone is wedged against a hydrophobic corner, and successive hydroxyl groups form hydrogen bonds with a pair of acceptor, and donor atoms. Two conserved aspartic acid-proline-alanine motifs form a key interface between two gene-duplicated segments that each encode three-and-one-half membrane-spanning helices around the channel. This structure elucidates the mechanism of selective permeability for linear carbohydrates and suggests how ions and water are excluded.

Department of Biochemistry and Biophysics, School of Medicine, University of California, San Francisco, CA 94143-0448, USA.
*   To whom correspondence should be addressed. E-mail: stroud{at}msg.ucsf.edu

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An Aquaglyceroporin Is Abundantly Expressed Early in the Development of the Suspensor and the Embryo Proper of Loblolly Pine.
V. T. Ciavatta, R. Morillon, G. S. Pullman, M. J. Chrispeels, and J. Cairney (2001)
Plant Physiology 127, 1556-1567
   Abstract »    Full Text »    PDF »
The tobacco plasma membrane aquaporin NtAQP1.
F. Siefritz, A. Biela, M. Eckert, B. Otto, N. Uehlein, and R. Kaldenhoff (2001)
J. Exp. Bot. 52, 1953-1957
   Abstract »    Full Text »    PDF »
Highly selective water channel activity measured by voltage clamp: Analysis of planar lipid bilayers reconstituted with purified AqpZ.
P. Pohl, S. M. Saparov, M. J. Borgnia, and P. Agre (2001)
PNAS
   Abstract »    Full Text »    PDF »
The Complete Set of Genes Encoding Major Intrinsic Proteins in Arabidopsis Provides a Framework for a New Nomenclature for Major Intrinsic Proteins in Plants.
U. Johanson, M. Karlsson, I. Johansson, S. Gustavsson, S. Sjovall, L. Fraysse, A. R. Weig, and P. Kjellbom (2001)
Plant Physiology 126, 1358-1369
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The Calpha ---H{middle dot}{middle dot}{middle dot}O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions.
A. Senes, I. Ubarretxena-Belandia, and D. M. Engelman (2001)
PNAS 98, 9056-9061
   Abstract »    Full Text »    PDF »
Functional characterization of a microbial aquaglyceroporin.
A. Froger, J.-P. Rolland, P. Bron, V. Lagrée, F. L. Cahérec, S. Deschamps, J.-F. Hubert, I. Pellerin, D. Thomas, and C. Delamarche (2001)
Microbiology 147, 1129-1135
   Abstract »    Full Text »
Aquaporins Constitute a Large and Highly Divergent Protein Family in Maize.
F. Chaumont, F. Barrieu, E. Wojcik, M. J. Chrispeels, and R. Jung (2001)
Plant Physiology 125, 1206-1215
   Abstract »    Full Text »
Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli.
M. J. Borgnia and P. Agre (2001)
PNAS
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