Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states
A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk’s ε subunit i...
| Main Authors: | , , , , , , |
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| Format: | Article |
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eLife Sciences Publications Ltd
2016-12-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/21598 |
| _version_ | 1811200688742465536 |
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| author | Meghna Sobti Callum Smits Andrew SW Wong Robert Ishmukhametov Daniela Stock Sara Sandin Alastair G Stewart |
| author_facet | Meghna Sobti Callum Smits Andrew SW Wong Robert Ishmukhametov Daniela Stock Sara Sandin Alastair G Stewart |
| author_sort | Meghna Sobti |
| collection | DOAJ |
| description | A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk’s ε subunit in an extended autoinhibitory conformation in all three states. The Fo motor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex, revealing the F1 attachment points and a coiled-coil that bifurcates toward the membrane with its helices separating to embrace subunit a from two sides. |
| first_indexed | 2024-04-12T02:08:07Z |
| format | Article |
| id | doaj.art-a52703980fed4f21ade8137278f80129 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:08:07Z |
| publishDate | 2016-12-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-a52703980fed4f21ade8137278f801292022-12-22T03:52:29ZengeLife Sciences Publications LtdeLife2050-084X2016-12-01510.7554/eLife.21598Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational statesMeghna Sobti0Callum Smits1Andrew SW Wong2Robert Ishmukhametov3Daniela Stock4Sara Sandin5Alastair G Stewart6https://orcid.org/0000-0002-2070-6030Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, AustraliaMolecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, AustraliaNTU Institute of Structural Biology, Nanyang Technological University, Singapore, SingaporeDepartment of Physics, Clarendon Laboratory, University of Oxford, Oxford, United KingdomMolecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia; Faculty of Medicine, The University of New South Wales, Sydney, AustraliaNTU Institute of Structural Biology, Nanyang Technological University, Singapore, Singapore; School of Biological Sciences, Nanyang Technological University, Singapore, SingaporeMolecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia; Faculty of Medicine, The University of New South Wales, Sydney, AustraliaA molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk’s ε subunit in an extended autoinhibitory conformation in all three states. The Fo motor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex, revealing the F1 attachment points and a coiled-coil that bifurcates toward the membrane with its helices separating to embrace subunit a from two sides.https://elifesciences.org/articles/21598ATP synthaserotary ATPasecryoEMbioenergeticsmembrane protein |
| spellingShingle | Meghna Sobti Callum Smits Andrew SW Wong Robert Ishmukhametov Daniela Stock Sara Sandin Alastair G Stewart Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states eLife ATP synthase rotary ATPase cryoEM bioenergetics membrane protein |
| title | Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states |
| title_full | Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states |
| title_fullStr | Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states |
| title_full_unstemmed | Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states |
| title_short | Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states |
| title_sort | cryo em structures of the autoinhibited e coli atp synthase in three rotational states |
| topic | ATP synthase rotary ATPase cryoEM bioenergetics membrane protein |
| url | https://elifesciences.org/articles/21598 |
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