The three-dimensional structure of aquaporin-1

Thomas Walz, Teruhisa Hirai, Kazuyoshi Murata, J. Bernard Heymann, Kaoru Mitsuoka, Yoshinori Fujiyoshi, Barbara L. Smith, Peter Agre and Andreas Engel
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Thomas Walz: *M. E. Mller-Institute for Microscopic Structural Biology at the Biozentrum, University of Basel
Teruhisa Hirai: ‡International Institute for Advanced Research, Matsushita Electric Industrial Co., Ltd.
Kazuyoshi Murata: ‡International Institute for Advanced Research, Matsushita Electric Industrial Co., Ltd.
J. Bernard Heymann: *M. E. Mller-Institute for Microscopic Structural Biology at the Biozentrum, University of Basel
Kaoru Mitsuoka: ‡International Institute for Advanced Research, Matsushita Electric Industrial Co., Ltd.
Yoshinori Fujiyoshi: Faculty of Science, Kyoto University, Kitashirakawa
Barbara L. Smith: Johns Hopkins University School of Medicine
Peter Agre: Johns Hopkins University School of Medicine
Andreas Engel: *M. E. Mller-Institute for Microscopic Structural Biology at the Biozentrum, University of Basel

Nature, 1997, vol. 387, issue 6633, 624-627

Abstract: Abstract The entry and exit of water from cells is a fundamental process of life. Recognition of the high water permeability of red blood cells led to the proposal that specialized water pores exist in the plasma membrane1. Expression in Xenopus oocytes and functional studies of an erythrocyte integral membrane protein of relative molecular mass 28,000, identified it as the mercury-sensitive water channel, aquaporin-1 (AQP1)2. Many related proteins, all belonging to the major intrinsic protein (MIP) family, are found throughout nature3. AQP1 is a homotetramer containing four independent aqueous channels4,5,6. When reconstituted into lipid bilayers, the protein forms two-dimensional lattices with a unit cell containing two tetramers in opposite orientation7,8,9,10. Here we present the three-dimensional structure of AQP1 determined at 6Å resolution by cryo-electron microscopy. Each AQP1 monomer has six tilted, bilayer-spanning α-helices which form a right-handed bundle surrounding a central density. These results, together with functional studies, provide a model that identifies the aqueous pore in the AQP1 molecule and indicates the organization of the tetrameric complex in the membrane.

Date: 1997
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DOI: 10.1038/42512

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