Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F1–Fo coupling
Mitochondrial adenosine triphosphate (ATP) synthase uses the proton gradient across the inner mitochondrial membrane to synthesize ATP. Structural and single molecule studies conducted mostly at neutral or basic pH have provided details of the reaction mechanism of ATP synthesis. However, pH of the...
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Veröffentlicht in: | Nature structural & molecular biology 2024-04, Vol.31 (4), p.657-666 |
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creator | Sharma, Stuti Luo, Min Patel, Hiral Mueller, David M. Liao, Maofu |
description | Mitochondrial adenosine triphosphate (ATP) synthase uses the proton gradient across the inner mitochondrial membrane to synthesize ATP. Structural and single molecule studies conducted mostly at neutral or basic pH have provided details of the reaction mechanism of ATP synthesis. However, pH of the mitochondrial matrix is slightly acidic during hypoxia and pH-dependent conformational changes in the ATP synthase have been reported. Here we use single-particle cryo-EM to analyze the conformational ensemble of the yeast (
Saccharomyces cerevisiae
) ATP synthase at pH 6. Of the four conformations resolved in this study, three are reaction intermediates. In addition to canonical catalytic dwell and binding dwell structures, we identify two unique conformations with nearly identical positions of the central rotor but different catalytic site conformations. These structures provide new insights into the catalytic mechanism of the ATP synthase and highlight elastic coupling between the catalytic and proton translocating domains.
Here the authors determined structures of the mitochondrial ATP synthase at pH 6, in four distinct conformations. The structures represent intermediates in the reaction cycle of the enzyme and provide insights into its elastic coupling mechanism. |
doi_str_mv | 10.1038/s41594-024-01219-4 |
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Saccharomyces cerevisiae
) ATP synthase at pH 6. Of the four conformations resolved in this study, three are reaction intermediates. In addition to canonical catalytic dwell and binding dwell structures, we identify two unique conformations with nearly identical positions of the central rotor but different catalytic site conformations. These structures provide new insights into the catalytic mechanism of the ATP synthase and highlight elastic coupling between the catalytic and proton translocating domains.
Here the authors determined structures of the mitochondrial ATP synthase at pH 6, in four distinct conformations. The structures represent intermediates in the reaction cycle of the enzyme and provide insights into its elastic coupling mechanism.</description><identifier>ISSN: 1545-9993</identifier><identifier>ISSN: 1545-9985</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/s41594-024-01219-4</identifier><identifier>PMID: 38316880</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/45/612/1237 ; 631/45/612/1240 ; 631/535/1258/1259 ; Adenosine triphosphate ; ATP ; ATP synthase ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Chemical synthesis ; Coupling ; Hypoxia ; Intermediates ; Life Sciences ; Membrane Biology ; Mitochondria ; pH effects ; Protein Structure ; Protons ; Reaction intermediates ; Reaction mechanisms ; Yeast ; Yeasts</subject><ispartof>Nature structural & molecular biology, 2024-04, Vol.31 (4), p.657-666</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2024. The Author(s), under exclusive licence to Springer Nature America, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c359t-985a78c048e492be610b407f602247695134b98ff79ffdd6431270a5c4b3bef93</cites><orcidid>0000-0002-1478-0445 ; 0000-0002-3481-450X ; 0000-0002-1180-0287</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids></links><search><creatorcontrib>Sharma, Stuti</creatorcontrib><creatorcontrib>Luo, Min</creatorcontrib><creatorcontrib>Patel, Hiral</creatorcontrib><creatorcontrib>Mueller, David M.</creatorcontrib><creatorcontrib>Liao, Maofu</creatorcontrib><title>Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F1–Fo coupling</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><description>Mitochondrial adenosine triphosphate (ATP) synthase uses the proton gradient across the inner mitochondrial membrane to synthesize ATP. Structural and single molecule studies conducted mostly at neutral or basic pH have provided details of the reaction mechanism of ATP synthesis. However, pH of the mitochondrial matrix is slightly acidic during hypoxia and pH-dependent conformational changes in the ATP synthase have been reported. Here we use single-particle cryo-EM to analyze the conformational ensemble of the yeast (
Saccharomyces cerevisiae
) ATP synthase at pH 6. Of the four conformations resolved in this study, three are reaction intermediates. In addition to canonical catalytic dwell and binding dwell structures, we identify two unique conformations with nearly identical positions of the central rotor but different catalytic site conformations. These structures provide new insights into the catalytic mechanism of the ATP synthase and highlight elastic coupling between the catalytic and proton translocating domains.
Here the authors determined structures of the mitochondrial ATP synthase at pH 6, in four distinct conformations. The structures represent intermediates in the reaction cycle of the enzyme and provide insights into its elastic coupling mechanism.</description><subject>631/45/612/1237</subject><subject>631/45/612/1240</subject><subject>631/535/1258/1259</subject><subject>Adenosine triphosphate</subject><subject>ATP</subject><subject>ATP synthase</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Chemical synthesis</subject><subject>Coupling</subject><subject>Hypoxia</subject><subject>Intermediates</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Mitochondria</subject><subject>pH effects</subject><subject>Protein Structure</subject><subject>Protons</subject><subject>Reaction intermediates</subject><subject>Reaction mechanisms</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>1545-9993</issn><issn>1545-9985</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNp9kU1uFDEQhS0EIiFwAVaW2LBp8G-3vULRiCFIkWAR1pa7pzxx5LYb251odtyBG3ISDBMFwYKFVZbqe09V9RB6SckbSrh6WwSVWnSEtUcZ1Z14hE6pFLLTWsnHD3_NT9CzUm4IYVIO_Ck64YrTXilyiu42KbqUZ1t9ijZgiAXmMQBODh_AlorPrz7jcoj12hbAtuKQ7vBygTPcgg0Fr9F_XQH7WCHPsPO2QsE27vASmtpPvh5aE2_pj2_ftwlPaV2Cj_vn6IlrcnhxX8_Ql-37q81Fd_npw8fN-WU3calr1_awg5qIUCA0G6GnZBRkcD1hTAy9lpSLUSvnBu3cbtcLTtlArJzEyEdwmp-hd0ffZR3beBPEmm0wS_azzQeTrDd_d6K_Nvt0a2g7HqNENofX9w45tU1LNbMvE4RgI6S1GKYZ02KQUjX01T_oTVpzO2sxnAhKKB0kaxQ7UlNOpWRwD9NQYn4Fa47Bmhas-R2sEU3Ej6LS4LiH_Mf6P6qfLyCmfA</recordid><startdate>20240401</startdate><enddate>20240401</enddate><creator>Sharma, Stuti</creator><creator>Luo, Min</creator><creator>Patel, Hiral</creator><creator>Mueller, David M.</creator><creator>Liao, Maofu</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-1478-0445</orcidid><orcidid>https://orcid.org/0000-0002-3481-450X</orcidid><orcidid>https://orcid.org/0000-0002-1180-0287</orcidid></search><sort><creationdate>20240401</creationdate><title>Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F1–Fo coupling</title><author>Sharma, Stuti ; 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Structural and single molecule studies conducted mostly at neutral or basic pH have provided details of the reaction mechanism of ATP synthesis. However, pH of the mitochondrial matrix is slightly acidic during hypoxia and pH-dependent conformational changes in the ATP synthase have been reported. Here we use single-particle cryo-EM to analyze the conformational ensemble of the yeast (
Saccharomyces cerevisiae
) ATP synthase at pH 6. Of the four conformations resolved in this study, three are reaction intermediates. In addition to canonical catalytic dwell and binding dwell structures, we identify two unique conformations with nearly identical positions of the central rotor but different catalytic site conformations. These structures provide new insights into the catalytic mechanism of the ATP synthase and highlight elastic coupling between the catalytic and proton translocating domains.
Here the authors determined structures of the mitochondrial ATP synthase at pH 6, in four distinct conformations. The structures represent intermediates in the reaction cycle of the enzyme and provide insights into its elastic coupling mechanism.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>38316880</pmid><doi>10.1038/s41594-024-01219-4</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0002-1478-0445</orcidid><orcidid>https://orcid.org/0000-0002-3481-450X</orcidid><orcidid>https://orcid.org/0000-0002-1180-0287</orcidid></addata></record> |
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subjects | 631/45/612/1237 631/45/612/1240 631/535/1258/1259 Adenosine triphosphate ATP ATP synthase Biochemistry Biological Microscopy Biomedical and Life Sciences Chemical synthesis Coupling Hypoxia Intermediates Life Sciences Membrane Biology Mitochondria pH effects Protein Structure Protons Reaction intermediates Reaction mechanisms Yeast Yeasts |
title | Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F1–Fo coupling |
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