The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL
Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two back-to-back seven-membered rings of GroEL plays an important role in regulating binding and release o...
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| Veröffentlicht in: | Cell 1996-10, Vol.87 (2), p.241-251 |
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| creator | Roseman, Alan M Chen, Shaoxia White, Helen Braig, Kerstin Saibil, Helen R |
| description | Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two back-to-back seven-membered rings of GroEL plays an important role in regulating binding and release of folding substrates and of the small chaperonin GroES. Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 Å resolution for GroEL and GroEL–GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP. Nucleotide binding to the equatorial domains of GroEL causes large rotations of the apical domains, containing the GroES and substrate protein–binding sites. We propose a mechanism for allosteric switching and describe conformational changes that may be involved in critical steps of folding for substrates encapsulated by GroES. |
| doi_str_mv | 10.1016/S0092-8674(00)81342-2 |
| format | Article |
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Interaction between the two back-to-back seven-membered rings of GroEL plays an important role in regulating binding and release of folding substrates and of the small chaperonin GroES. Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 Å resolution for GroEL and GroEL–GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP. Nucleotide binding to the equatorial domains of GroEL causes large rotations of the apical domains, containing the GroES and substrate protein–binding sites. 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We propose a mechanism for allosteric switching and describe conformational changes that may be involved in critical steps of folding for substrates encapsulated by GroES.</description><subject>Adenosine Triphosphatases - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Allosteric Regulation</subject><subject>Bacterial Proteins - physiology</subject><subject>Binding Sites</subject><subject>Chaperonin 10 - physiology</subject><subject>Chaperonin 60 - physiology</subject><subject>Escherichia coli</subject><subject>Macromolecular Substances</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Movement</subject><subject>Protein Structure, Tertiary</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9vEzEQxS0EKmnhI1TyCcFhYfxnvQ4XFEIpSKlASjhbtneWGO3aqb0p6rfvpol67Wmkeb-ZJ71HyCWDjwyY-rQGmPNKq0a-B_igmZC84i_IjMG8qSRr-Esye0Jek_NS_gGAruv6jJxprdgc9IzkzRbpcmt3mFMMkS42v22ZNve-x8_0Bv3WxlAGmjq66PtURszB0_X_MPptiH-pjS29SXc4YBzLgVrvXRmzHbH6GmJ7QL6lwYZY6PT9Oqer1RvyqrN9wbeneUH-fL_aLH9Uq1_XP5eLVeVrkGMlhfKtEko0TivOhHfQ2cZZ5pUTUCsvEOZSOSc75K21Ummn-cR0njOnmLgg745_dznd7rGMZgjFY9_biGlfTKMlb7RongVZrbRSWk5gfQR9TqVk7Mwuh8Hme8PAHEoxj6WYQ-IGwDyWYvh0d3ky2LsB26erUwuT_uWo4xTHXcBsig8YPbYhox9Nm8IzDg9AX5v8</recordid><startdate>19961018</startdate><enddate>19961018</enddate><creator>Roseman, Alan M</creator><creator>Chen, Shaoxia</creator><creator>White, Helen</creator><creator>Braig, Kerstin</creator><creator>Saibil, Helen R</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>C1K</scope><scope>7X8</scope></search><sort><creationdate>19961018</creationdate><title>The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL</title><author>Roseman, Alan M ; Chen, Shaoxia ; White, Helen ; Braig, Kerstin ; Saibil, Helen R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-436cd63637b86213cb0fa7ba1c6b3056c3e0946bb4fe2daa468b820fafc21b613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Adenosine Triphosphatases - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Allosteric Regulation</topic><topic>Bacterial Proteins - physiology</topic><topic>Binding Sites</topic><topic>Chaperonin 10 - physiology</topic><topic>Chaperonin 60 - physiology</topic><topic>Escherichia coli</topic><topic>Macromolecular Substances</topic><topic>Microscopy, Electron</topic><topic>Models, Molecular</topic><topic>Movement</topic><topic>Protein Structure, Tertiary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Roseman, Alan M</creatorcontrib><creatorcontrib>Chen, Shaoxia</creatorcontrib><creatorcontrib>White, Helen</creatorcontrib><creatorcontrib>Braig, Kerstin</creatorcontrib><creatorcontrib>Saibil, Helen R</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Roseman, Alan M</au><au>Chen, Shaoxia</au><au>White, Helen</au><au>Braig, Kerstin</au><au>Saibil, Helen R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1996-10-18</date><risdate>1996</risdate><volume>87</volume><issue>2</issue><spage>241</spage><epage>251</epage><pages>241-251</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two back-to-back seven-membered rings of GroEL plays an important role in regulating binding and release of folding substrates and of the small chaperonin GroES. Using cryo-electron microscopy, we have obtained three-dimensional reconstructions to 30 Å resolution for GroEL and GroEL–GroES complexes in the presence of ADP, ATP, and the nonhydrolyzable ATP analog, AMP-PNP. Nucleotide binding to the equatorial domains of GroEL causes large rotations of the apical domains, containing the GroES and substrate protein–binding sites. We propose a mechanism for allosteric switching and describe conformational changes that may be involved in critical steps of folding for substrates encapsulated by GroES.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8861908</pmid><doi>10.1016/S0092-8674(00)81342-2</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; EZB-FREE-00999 freely available EZB journals |
| subjects | Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Allosteric Regulation Bacterial Proteins - physiology Binding Sites Chaperonin 10 - physiology Chaperonin 60 - physiology Escherichia coli Macromolecular Substances Microscopy, Electron Models, Molecular Movement Protein Structure, Tertiary |
| title | The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL |
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