Structural determinants of water permeation through aquaporin-1
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 aqueo...
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| Veröffentlicht in: | Nature (London) 2000-10, Vol.407 (6804), p.599-605 |
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| creator | Murata, Kazuyoshi Mitsuoka, Kaoru Hirai, Teruhisa Walz, Thomas Agre, Peter Heymann, J. Bernard Engel, Andreas Fujiyoshi, Yoshinori |
| description | 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. |
| doi_str_mv | 10.1038/35036519 |
| format | Article |
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Bernard ; Engel, Andreas ; Fujiyoshi, Yoshinori</creator><creatorcontrib>Murata, Kazuyoshi ; Mitsuoka, Kaoru ; Hirai, Teruhisa ; Walz, Thomas ; Agre, Peter ; Heymann, J. Bernard ; Engel, Andreas ; Fujiyoshi, Yoshinori</creatorcontrib><description>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.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/35036519</identifier><identifier>PMID: 11034202</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Amino acids ; Anatomy & physiology ; Aquaporin 1 ; Aquaporins - chemistry ; Biological and medical sciences ; Cell Membrane Permeability ; Cell physiology ; Cells ; Crystallography - methods ; Electrons ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; Membrane and intracellular transports ; Membranes ; Models, Molecular ; Molecular and cellular biology ; Molecular biology ; Molecular Sequence Data ; multidisciplinary ; Permeability ; Protein Conformation ; Protein Folding ; Protons ; Science ; Science (multidisciplinary) ; Water ; Water - chemistry ; Water transport</subject><ispartof>Nature (London), 2000-10, Vol.407 (6804), p.599-605</ispartof><rights>Macmillan Magazines Ltd. 2000</rights><rights>2001 INIST-CNRS</rights><rights>COPYRIGHT 2000 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. 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Bernard</creatorcontrib><creatorcontrib>Engel, Andreas</creatorcontrib><creatorcontrib>Fujiyoshi, Yoshinori</creatorcontrib><title>Structural determinants of water permeation through aquaporin-1</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>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.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Anatomy & physiology</subject><subject>Aquaporin 1</subject><subject>Aquaporins - chemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane Permeability</subject><subject>Cell physiology</subject><subject>Cells</subject><subject>Crystallography - methods</subject><subject>Electrons</subject><subject>Fundamental and applied biological sciences. 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Bernard</au><au>Engel, Andreas</au><au>Fujiyoshi, Yoshinori</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural determinants of water permeation through aquaporin-1</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2000-10-05</date><risdate>2000</risdate><volume>407</volume><issue>6804</issue><spage>599</spage><epage>605</epage><pages>599-605</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><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.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>11034202</pmid><doi>10.1038/35036519</doi><tpages>7</tpages></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Anatomy & physiology Aquaporin 1 Aquaporins - chemistry Biological and medical sciences Cell Membrane Permeability Cell physiology Cells Crystallography - methods Electrons Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Membrane and intracellular transports Membranes Models, Molecular Molecular and cellular biology Molecular biology Molecular Sequence Data multidisciplinary Permeability Protein Conformation Protein Folding Protons Science Science (multidisciplinary) Water Water - chemistry Water transport |
| title | Structural determinants of water permeation through aquaporin-1 |
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