Structure of a bacterial ATP synthase
ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expr...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2019-02-01
|
| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/43128 |
| _version_ | 1811181129642803200 |
|---|---|
| author | Hui Guo Toshiharu Suzuki John L Rubinstein |
| author_facet | Hui Guo Toshiharu Suzuki John L Rubinstein |
| author_sort | Hui Guo |
| collection | DOAJ |
| description | ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit ε shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme. |
| first_indexed | 2024-04-11T09:13:24Z |
| format | Article |
| id | doaj.art-035c14f858f8430c81a9ae7f4de7605a |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:13:24Z |
| publishDate | 2019-02-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-035c14f858f8430c81a9ae7f4de7605a2022-12-22T04:32:25ZengeLife Sciences Publications LtdeLife2050-084X2019-02-01810.7554/eLife.43128Structure of a bacterial ATP synthaseHui Guo0https://orcid.org/0000-0001-7007-2876Toshiharu Suzuki1John L Rubinstein2https://orcid.org/0000-0003-0566-2209The Hospital for Sick Children Research Institute, Toronto, Canada; Department of Medical Biophysics, The University of Toronto, Toronto, CanadaLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan; Department of Molecular Bioscience, Kyoto-Sangyo University, Kyoto, JapanThe Hospital for Sick Children Research Institute, Toronto, Canada; Department of Medical Biophysics, The University of Toronto, Toronto, Canada; Department of Biochemistry, The University of Toronto, Toronto, CanadaATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit ε shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme.https://elifesciences.org/articles/43128ATP synthaseBacillus PS3membraneproteinstructurecryo-EM |
| spellingShingle | Hui Guo Toshiharu Suzuki John L Rubinstein Structure of a bacterial ATP synthase eLife ATP synthase Bacillus PS3 membrane protein structure cryo-EM |
| title | Structure of a bacterial ATP synthase |
| title_full | Structure of a bacterial ATP synthase |
| title_fullStr | Structure of a bacterial ATP synthase |
| title_full_unstemmed | Structure of a bacterial ATP synthase |
| title_short | Structure of a bacterial ATP synthase |
| title_sort | structure of a bacterial atp synthase |
| topic | ATP synthase Bacillus PS3 membrane protein structure cryo-EM |
| url | https://elifesciences.org/articles/43128 |
| work_keys_str_mv | AT huiguo structureofabacterialatpsynthase AT toshiharusuzuki structureofabacterialatpsynthase AT johnlrubinstein structureofabacterialatpsynthase |