The aerolysin membrane channel is formed by heptamerization of the monomer
The cytolytic toxin aerolysin has been found to form heptameric oligomers by SDS‐PAGE electrophoresis, STEM mass measurements of single oligomers and image analysis of two‐dimensional membrane crystals. Two types of crystal, flat sheets and long regular tubes, have been obtained by reconstitution of...
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| Veröffentlicht in: | The EMBO journal 1992-07, Vol.11 (7), p.2457-2463 |
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| creator | Wilmsen, H.U. Leonard, K.R. Tichelaar, W. Buckley, J.T. Pattus, F. |
| description | The cytolytic toxin aerolysin has been found to form heptameric oligomers by SDS‐PAGE electrophoresis, STEM mass measurements of single oligomers and image analysis of two‐dimensional membrane crystals. Two types of crystal, flat sheets and long regular tubes, have been obtained by reconstitution of purified protein and Escherichia coli phospholipids. A noise‐filtered image of the best crystalline sheets reveals a structure with 7‐fold symmetry containing a central strongly stain‐excluding ring that encircles a dark stain‐filled channel 17 A in diameter. The ring is surrounded by seven arms each made up of two unequal sized domains. By combining projected views and side‐views, a simplified model of the aerolysin channel complex has been constructed. The relevance of this structure to the mode of action of aerolysin is discussed. |
| doi_str_mv | 10.1002/j.1460-2075.1992.tb05310.x |
| format | Article |
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Two types of crystal, flat sheets and long regular tubes, have been obtained by reconstitution of purified protein and Escherichia coli phospholipids. A noise‐filtered image of the best crystalline sheets reveals a structure with 7‐fold symmetry containing a central strongly stain‐excluding ring that encircles a dark stain‐filled channel 17 A in diameter. The ring is surrounded by seven arms each made up of two unequal sized domains. By combining projected views and side‐views, a simplified model of the aerolysin channel complex has been constructed. The relevance of this structure to the mode of action of aerolysin is discussed.</description><subject>aerolysin</subject><subject>Aeromonas hydrophila</subject><subject>Bacterial Toxins - chemistry</subject><subject>Biological and medical sciences</subject><subject>crystal structure</subject><subject>Crystalline structure</subject><subject>electron microscopy</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - metabolism</subject><subject>formation</subject><subject>Fourier Analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Image Processing, Computer-Assisted</subject><subject>Ion Channels - chemistry</subject><subject>Ion Channels - ultrastructure</subject><subject>membrane channels</subject><subject>Microscopy, Electron</subject><subject>Molecular biophysics</subject><subject>Molecular Weight</subject><subject>Phospholipids - chemistry</subject><subject>Polymers</subject><subject>Pore Forming Cytotoxic Proteins</subject><subject>Structure in molecular biology</subject><subject>Trypsin</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkUFv1DAQhS0EKkvhJyBZCHHLMk5sx0HiUKpCqYq4lLNlOxPWqyRe7Cx0-fU47GoLp6onW37vWW_mI-QVgyUDKN-ul4xLKEqoxZI1TbmcLIgqq7ePyOIoPSYLKCUrOFPNU_IspTUACFWzE3LCqlpVDSzI1c0KqcEY-l3yIx1wsNGMSN3KjCP21CfahThgS-2OrnAzmQGj_20mH0YaOjrl-BDGkF-fkyed6RO-OJyn5NvHi5vzy-L666fP52fXhZPAoRCdFV0L0nFrjVOS24YxJ5RyruTOGJDIW4fAWisUr7BlCFI2SrpWtp3oqlPyfv_vZmtzMYfjFE2vN9EPJu50MF7_r4x-pb-Hn1oIWZeQ828O-Rh-bDFNevDJYd_nucM26bqCmuVF3WtkshS1qmfju73RxZBSxO5YhoGeiem1nrHoGYueiekDMX2bwy__HecuukeU9dcH3SRn-i7jcT4dbaISjeCz7Wxv--V73D2ggL748uHq7736A_8WtbM</recordid><startdate>199207</startdate><enddate>199207</enddate><creator>Wilmsen, H.U.</creator><creator>Leonard, K.R.</creator><creator>Tichelaar, W.</creator><creator>Buckley, J.T.</creator><creator>Pattus, F.</creator><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>199207</creationdate><title>The aerolysin membrane channel is formed by heptamerization of the monomer</title><author>Wilmsen, H.U. ; Leonard, K.R. ; Tichelaar, W. ; Buckley, J.T. ; Pattus, F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6040-5fb5fd06c4bbac864b911c588cc24caa06e4dce01db5843ed1e066986cd6df5f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>aerolysin</topic><topic>Aeromonas hydrophila</topic><topic>Bacterial Toxins - chemistry</topic><topic>Biological and medical sciences</topic><topic>crystal structure</topic><topic>Crystalline structure</topic><topic>electron microscopy</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - metabolism</topic><topic>formation</topic><topic>Fourier Analysis</topic><topic>Fundamental and applied biological sciences. 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Two types of crystal, flat sheets and long regular tubes, have been obtained by reconstitution of purified protein and Escherichia coli phospholipids. A noise‐filtered image of the best crystalline sheets reveals a structure with 7‐fold symmetry containing a central strongly stain‐excluding ring that encircles a dark stain‐filled channel 17 A in diameter. The ring is surrounded by seven arms each made up of two unequal sized domains. By combining projected views and side‐views, a simplified model of the aerolysin channel complex has been constructed. The relevance of this structure to the mode of action of aerolysin is discussed.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>1378390</pmid><doi>10.1002/j.1460-2075.1992.tb05310.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | aerolysin Aeromonas hydrophila Bacterial Toxins - chemistry Biological and medical sciences crystal structure Crystalline structure electron microscopy Electrophoresis, Polyacrylamide Gel Escherichia coli - metabolism formation Fourier Analysis Fundamental and applied biological sciences. Psychology Image Processing, Computer-Assisted Ion Channels - chemistry Ion Channels - ultrastructure membrane channels Microscopy, Electron Molecular biophysics Molecular Weight Phospholipids - chemistry Polymers Pore Forming Cytotoxic Proteins Structure in molecular biology Trypsin |
| title | The aerolysin membrane channel is formed by heptamerization of the monomer |
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