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: | Journal Article |
| Language: | English |
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2018
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| Online Access: | https://hdl.handle.net/10356/89777 http://hdl.handle.net/10220/46435 |
| _version_ | 1811691008495190016 |
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| author | Sobti, Meghna Smits, Callum Ishmukhametov, Robert Stock, Daniela Sandin, Sara Stewart, Alastair G Wong, Andrew See Weng |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Sobti, Meghna Smits, Callum Ishmukhametov, Robert Stock, Daniela Sandin, Sara Stewart, Alastair G Wong, Andrew See Weng |
| author_sort | Sobti, Meghna |
| collection | NTU |
| 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 | 2024-10-01T06:13:04Z |
| format | Journal Article |
| id | ntu-10356/89777 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T06:13:04Z |
| publishDate | 2018 |
| record_format | dspace |
| spelling | ntu-10356/897772023-02-28T17:04:02Z Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states Sobti, Meghna Smits, Callum Ishmukhametov, Robert Stock, Daniela Sandin, Sara Stewart, Alastair G Wong, Andrew See Weng School of Biological Sciences NTU Institute of Structural Biology Cryo-EM E. Coli ATP Synthase DRNTU::Science::Biological sciences 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. MOE (Min. of Education, S’pore) Published version 2018-10-26T01:27:06Z 2019-12-06T17:33:15Z 2018-10-26T01:27:06Z 2019-12-06T17:33:15Z 2016 Journal Article Sobti, M., Smits, C., Wong, A. S. W., Ishmukhametov, R., Stock, D., Sandin, S., & Stewart, A. G. (2016). Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states. eLife, 5, e21598-. doi:10.7554/eLife.21598 https://hdl.handle.net/10356/89777 http://hdl.handle.net/10220/46435 10.7554/eLife.21598 en eLife © Sobti et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited. 18 p. application/pdf |
| spellingShingle | Cryo-EM E. Coli ATP Synthase DRNTU::Science::Biological sciences Sobti, Meghna Smits, Callum Ishmukhametov, Robert Stock, Daniela Sandin, Sara Stewart, Alastair G Wong, Andrew See Weng Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states |
| 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 | Cryo-EM E. Coli ATP Synthase DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/89777 http://hdl.handle.net/10220/46435 |
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