Open channel structure of MscL and the gating mechanism of mechanosensitive channels
Mechanosensitive channels act as membrane-embedded mechano-electrical switches, opening a large water-filled pore in response to lipid bilayer deformations. This process is critical to the response of living organisms to direct physical stimulation, such as in touch, hearing and osmoregulation. Here...
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| Veröffentlicht in: | Nature (London) 2002-08, Vol.418 (6901), p.942-948 |
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| creator | Perozo, Eduardo Cortes, D. Marien Sompornpisut, Pornthep Kloda, Anna Martinac, Boris |
| description | Mechanosensitive channels act as membrane-embedded mechano-electrical switches, opening a large water-filled pore in response to lipid bilayer deformations. This process is critical to the response of living organisms to direct physical stimulation, such as in touch, hearing and osmoregulation. Here, we have determined the structural rearrangements that underlie these events in the large prokaryotic mechanosensitive channel (MscL) using electron paramagnetic resonance spectroscopy and site-directed spin labelling. MscL was trapped in both the open and in an intermediate closed state by modulating bilayer morphology. Transition to the intermediate state is characterized by small movements in the first transmembrane helix (TM1). Subsequent transitions to the open state are accompanied by massive rearrangements in both TM1 and TM2, as shown by large increases in probe dynamics, solvent accessibility and the elimination of all intersubunit spin-spin interactions. The open state is highly dynamic, supporting a water-filled pore of at least 25 A, lined mostly by TM1. These structures suggest a plausible molecular mechanism of gating in mechanosensitive channels. |
| doi_str_mv | 10.1038/nature00992 |
| format | Article |
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Subsequent transitions to the open state are accompanied by massive rearrangements in both TM1 and TM2, as shown by large increases in probe dynamics, solvent accessibility and the elimination of all intersubunit spin-spin interactions. The open state is highly dynamic, supporting a water-filled pore of at least 25 A, lined mostly by TM1. These structures suggest a plausible molecular mechanism of gating in mechanosensitive channels.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature00992</identifier><identifier>PMID: 12198539</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing</publisher><subject>Biological and medical sciences ; Cell membranes. Ionic channels. Membrane pores ; Cell structures and functions ; Computer Simulation ; Crystal structure ; Crystals ; Cysteine - genetics ; Cysteine - metabolism ; Electron Spin Resonance Spectroscopy ; Escherichia coli Proteins ; Fundamental and applied biological sciences. Psychology ; Ion Channel Gating ; Ion Channels - chemistry ; Ion Channels - genetics ; Ion Channels - metabolism ; Lipid Bilayers - chemistry ; Lipid Bilayers - metabolism ; Lipids ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membranes ; Models, Molecular ; Molecular and cellular biology ; Molecular biology ; Open channels ; Osmoregulation ; Protein Structure, Quaternary ; Solvents ; Space life sciences ; Spectrum analysis ; Spin Labels ; Thermodynamics</subject><ispartof>Nature (London), 2002-08, Vol.418 (6901), p.942-948</ispartof><rights>2002 INIST-CNRS</rights><rights>COPYRIGHT 2002 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. 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Transition to the intermediate state is characterized by small movements in the first transmembrane helix (TM1). Subsequent transitions to the open state are accompanied by massive rearrangements in both TM1 and TM2, as shown by large increases in probe dynamics, solvent accessibility and the elimination of all intersubunit spin-spin interactions. The open state is highly dynamic, supporting a water-filled pore of at least 25 A, lined mostly by TM1. These structures suggest a plausible molecular mechanism of gating in mechanosensitive channels.</description><subject>Biological and medical sciences</subject><subject>Cell membranes. Ionic channels. 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Marien</au><au>Sompornpisut, Pornthep</au><au>Kloda, Anna</au><au>Martinac, Boris</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Open channel structure of MscL and the gating mechanism of mechanosensitive channels</atitle><jtitle>Nature (London)</jtitle><addtitle>Nature</addtitle><date>2002-08-29</date><risdate>2002</risdate><volume>418</volume><issue>6901</issue><spage>942</spage><epage>948</epage><pages>942-948</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Mechanosensitive channels act as membrane-embedded mechano-electrical switches, opening a large water-filled pore in response to lipid bilayer deformations. This process is critical to the response of living organisms to direct physical stimulation, such as in touch, hearing and osmoregulation. Here, we have determined the structural rearrangements that underlie these events in the large prokaryotic mechanosensitive channel (MscL) using electron paramagnetic resonance spectroscopy and site-directed spin labelling. MscL was trapped in both the open and in an intermediate closed state by modulating bilayer morphology. Transition to the intermediate state is characterized by small movements in the first transmembrane helix (TM1). Subsequent transitions to the open state are accompanied by massive rearrangements in both TM1 and TM2, as shown by large increases in probe dynamics, solvent accessibility and the elimination of all intersubunit spin-spin interactions. The open state is highly dynamic, supporting a water-filled pore of at least 25 A, lined mostly by TM1. These structures suggest a plausible molecular mechanism of gating in mechanosensitive channels.</abstract><cop>London</cop><pub>Nature Publishing</pub><pmid>12198539</pmid><doi>10.1038/nature00992</doi><tpages>7</tpages></addata></record> |
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| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | Biological and medical sciences Cell membranes. Ionic channels. Membrane pores Cell structures and functions Computer Simulation Crystal structure Crystals Cysteine - genetics Cysteine - metabolism Electron Spin Resonance Spectroscopy Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Ion Channel Gating Ion Channels - chemistry Ion Channels - genetics Ion Channels - metabolism Lipid Bilayers - chemistry Lipid Bilayers - metabolism Lipids Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Membranes Models, Molecular Molecular and cellular biology Molecular biology Open channels Osmoregulation Protein Structure, Quaternary Solvents Space life sciences Spectrum analysis Spin Labels Thermodynamics |
| title | Open channel structure of MscL and the gating mechanism of mechanosensitive channels |
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