Structural model of F1–ATPase and the implications for rotary catalysis
The crystal structure of bovine mitochondrial F1-ATPase is described. Several features of the structure are consistent with the binding change mechanism of catalysis, in which binding of substrates induces conformational changes that result in a high degree of cooperativity between the three catalyt...
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| Veröffentlicht in: | Philosophical transactions of the Royal Society of London. Series B. Biological sciences 2000-04, Vol.355 (1396), p.465-471 |
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| container_end_page | 471 |
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| container_title | Philosophical transactions of the Royal Society of London. Series B. Biological sciences |
| container_volume | 355 |
| creator | Leslie, A. G. W. Walker, J. E. |
| description | The crystal structure of bovine mitochondrial F1-ATPase is described. Several features of the structure are consistent with the binding change mechanism of catalysis, in which binding of substrates induces conformational changes that result in a high degree of cooperativity between the three catalytic sites. Furthermore, the structure also suggests that catalysis is accompanied by a physical rotation of the centrally placed γ-subunit relative to the approximately spherical α3β3 sub-assembly. |
| doi_str_mv | 10.1098/rstb.2000.0588 |
| format | Article |
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G. W. ; Walker, J. E.</creator><contributor>Huxley, A. F. ; Simmons, R. M. ; Huxley, A. F. ; Simmons, R. M.</contributor><creatorcontrib>Leslie, A. G. W. ; Walker, J. E. ; Huxley, A. F. ; Simmons, R. M. ; Huxley, A. F. ; Simmons, R. M.</creatorcontrib><description>The crystal structure of bovine mitochondrial F1-ATPase is described. Several features of the structure are consistent with the binding change mechanism of catalysis, in which binding of substrates induces conformational changes that result in a high degree of cooperativity between the three catalytic sites. Furthermore, the structure also suggests that catalysis is accompanied by a physical rotation of the centrally placed γ-subunit relative to the approximately spherical α3β3 sub-assembly.</description><identifier>ISSN: 0962-8436</identifier><identifier>EISSN: 1471-2970</identifier><identifier>DOI: 10.1098/rstb.2000.0588</identifier><identifier>PMID: 10836500</identifier><language>eng</language><publisher>England: The Royal Society</publisher><subject>Active sites ; Adenosine triphosphatases ; Animals ; Atpase ; Catalysis ; Cattle ; Crystal Structure ; Crystallography, X-Ray ; Enzymes ; F1-ATPase ; Hydrolysis ; Macromolecular Substances ; Mitochondria, Heart - enzymology ; Models, Molecular ; Nucleotides ; Protein Conformation ; Proton-Translocating ATPases - chemistry ; Proton-Translocating ATPases - metabolism ; Protons ; Rotary Catalysis ; Rotary Motors ; Rotation ; Ungulates</subject><ispartof>Philosophical transactions of the Royal Society of London. Series B. 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W.</creatorcontrib><creatorcontrib>Walker, J. E.</creatorcontrib><title>Structural model of F1–ATPase and the implications for rotary catalysis</title><title>Philosophical transactions of the Royal Society of London. Series B. Biological sciences</title><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><description>The crystal structure of bovine mitochondrial F1-ATPase is described. Several features of the structure are consistent with the binding change mechanism of catalysis, in which binding of substrates induces conformational changes that result in a high degree of cooperativity between the three catalytic sites. Furthermore, the structure also suggests that catalysis is accompanied by a physical rotation of the centrally placed γ-subunit relative to the approximately spherical α3β3 sub-assembly.</description><subject>Active sites</subject><subject>Adenosine triphosphatases</subject><subject>Animals</subject><subject>Atpase</subject><subject>Catalysis</subject><subject>Cattle</subject><subject>Crystal Structure</subject><subject>Crystallography, X-Ray</subject><subject>Enzymes</subject><subject>F1-ATPase</subject><subject>Hydrolysis</subject><subject>Macromolecular Substances</subject><subject>Mitochondria, Heart - enzymology</subject><subject>Models, Molecular</subject><subject>Nucleotides</subject><subject>Protein Conformation</subject><subject>Proton-Translocating ATPases - chemistry</subject><subject>Proton-Translocating ATPases - metabolism</subject><subject>Protons</subject><subject>Rotary Catalysis</subject><subject>Rotary Motors</subject><subject>Rotation</subject><subject>Ungulates</subject><issn>0962-8436</issn><issn>1471-2970</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9Uc1u1DAYtBCILoUrJ4Ry4pbFjv-SC6hUbFupEkgtXD85id31ksSL7QC58Q68IU-CQ8qqvXCy7G--mfEMQs8JXhNcla99iPW6wBivMS_LB2hFmCR5UUn8EK1wJYq8ZFQcoSch7BKq4pI9RkcEl1RwjFfo4ir6sYmjV13Wu1Z3mTPZhvz--evk-qMKOlNDm8Wtzmy_72yjonVDyIzzmXdR-SlLT6qbgg1P0SOjuqCf3Z7H6NPm_fXpeX754ezi9OQy3zJGY844Vo2iQnLNcMHKWkleFE1ZVEayVopWSl6XmrfENMa0WJBK1nXRFMYwLFRNj9GbhXc_1r1uGz3EZB723vbJDzhl4f5ksFu4cd-AiKqQAieCV7cE3n0ddYjQ29DorlODdmMASQhPIVYJ-PKu0kHiX3oJQBeAd1P6smusjhPs3OiHdE04mDuCuSOYO4K5o7T1Ytnahej8gZViISSeVfNlbEPUPw5j5b-AkFRy-FwyOD97R642JQeZ8G8X_NbebL9br-Gem7_ijRtiSgMo50BoJYAJDmbsUmytSQz4vwxu2ieOu7v0D2q4xdI</recordid><startdate>20000429</startdate><enddate>20000429</enddate><creator>Leslie, A. 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E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h443t-450aca3675e40248ba7522c829f74d76d775b8e5d1fcffd06197bb2c2ff406ab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Active sites</topic><topic>Adenosine triphosphatases</topic><topic>Animals</topic><topic>Atpase</topic><topic>Catalysis</topic><topic>Cattle</topic><topic>Crystal Structure</topic><topic>Crystallography, X-Ray</topic><topic>Enzymes</topic><topic>F1-ATPase</topic><topic>Hydrolysis</topic><topic>Macromolecular Substances</topic><topic>Mitochondria, Heart - enzymology</topic><topic>Models, Molecular</topic><topic>Nucleotides</topic><topic>Protein Conformation</topic><topic>Proton-Translocating ATPases - chemistry</topic><topic>Proton-Translocating ATPases - metabolism</topic><topic>Protons</topic><topic>Rotary Catalysis</topic><topic>Rotary Motors</topic><topic>Rotation</topic><topic>Ungulates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leslie, A. G. W.</creatorcontrib><creatorcontrib>Walker, J. E.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Philosophical transactions of the Royal Society of London. Series B. Biological sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leslie, A. G. W.</au><au>Walker, J. E.</au><au>Huxley, A. F.</au><au>Simmons, R. M.</au><au>Huxley, A. F.</au><au>Simmons, R. M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural model of F1–ATPase and the implications for rotary catalysis</atitle><jtitle>Philosophical transactions of the Royal Society of London. Series B. Biological sciences</jtitle><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><date>2000-04-29</date><risdate>2000</risdate><volume>355</volume><issue>1396</issue><spage>465</spage><epage>471</epage><pages>465-471</pages><issn>0962-8436</issn><eissn>1471-2970</eissn><abstract>The crystal structure of bovine mitochondrial F1-ATPase is described. Several features of the structure are consistent with the binding change mechanism of catalysis, in which binding of substrates induces conformational changes that result in a high degree of cooperativity between the three catalytic sites. Furthermore, the structure also suggests that catalysis is accompanied by a physical rotation of the centrally placed γ-subunit relative to the approximately spherical α3β3 sub-assembly.</abstract><cop>England</cop><pub>The Royal Society</pub><pmid>10836500</pmid><doi>10.1098/rstb.2000.0588</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0962-8436 |
| ispartof | Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 2000-04, Vol.355 (1396), p.465-471 |
| issn | 0962-8436 1471-2970 |
| language | eng |
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| source | MEDLINE; PubMed (Medline); JSTOR |
| subjects | Active sites Adenosine triphosphatases Animals Atpase Catalysis Cattle Crystal Structure Crystallography, X-Ray Enzymes F1-ATPase Hydrolysis Macromolecular Substances Mitochondria, Heart - enzymology Models, Molecular Nucleotides Protein Conformation Proton-Translocating ATPases - chemistry Proton-Translocating ATPases - metabolism Protons Rotary Catalysis Rotary Motors Rotation Ungulates |
| title | Structural model of F1–ATPase and the implications for rotary catalysis |
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