Structure and activation mechanism of the hexameric plasma membrane H+-ATPase
The plasma membrane H+ -ATPase is responsible for maintenance of the plasma membrane potential, which provides energy for the transport of nutrients, and the plasma membrane H+ -ATPase in S. cerevisiae (Pma1) is a P3A-type ATPase that assembles and functions as a hexamer. Here, the authors present t...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2021-11-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-26782-y |
| _version_ | 1819043751007354880 |
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| author | Peng Zhao Chaoran Zhao Dandan Chen Caihong Yun Huilin Li Lin Bai |
| author_facet | Peng Zhao Chaoran Zhao Dandan Chen Caihong Yun Huilin Li Lin Bai |
| author_sort | Peng Zhao |
| collection | DOAJ |
| description | The plasma membrane H+ -ATPase is responsible for maintenance of the plasma membrane potential, which provides energy for the transport of nutrients, and the plasma membrane H+ -ATPase in S. cerevisiae (Pma1) is a P3A-type ATPase that assembles and functions as a hexamer. Here, the authors present the cryo-EM structures of autoinhibited and activated native Pma1 hexamers purified with endogenous lipids and they propose a mechanism for proton pumping across the membrane by this family of H+ -ATPases. |
| first_indexed | 2024-12-21T10:01:45Z |
| format | Article |
| id | doaj.art-ef9f9738c0284bd28fc377cd31762f9f |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-21T10:01:45Z |
| publishDate | 2021-11-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-ef9f9738c0284bd28fc377cd31762f9f2022-12-21T19:07:55ZengNature PortfolioNature Communications2041-17232021-11-0112111110.1038/s41467-021-26782-yStructure and activation mechanism of the hexameric plasma membrane H+-ATPasePeng Zhao0Chaoran Zhao1Dandan Chen2Caihong Yun3Huilin Li4Lin Bai5Department of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking UniversityDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking UniversityDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking UniversityDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking UniversityDepartment of Structural Biology, Van Andel InstituteDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking UniversityThe plasma membrane H+ -ATPase is responsible for maintenance of the plasma membrane potential, which provides energy for the transport of nutrients, and the plasma membrane H+ -ATPase in S. cerevisiae (Pma1) is a P3A-type ATPase that assembles and functions as a hexamer. Here, the authors present the cryo-EM structures of autoinhibited and activated native Pma1 hexamers purified with endogenous lipids and they propose a mechanism for proton pumping across the membrane by this family of H+ -ATPases.https://doi.org/10.1038/s41467-021-26782-y |
| spellingShingle | Peng Zhao Chaoran Zhao Dandan Chen Caihong Yun Huilin Li Lin Bai Structure and activation mechanism of the hexameric plasma membrane H+-ATPase Nature Communications |
| title | Structure and activation mechanism of the hexameric plasma membrane H+-ATPase |
| title_full | Structure and activation mechanism of the hexameric plasma membrane H+-ATPase |
| title_fullStr | Structure and activation mechanism of the hexameric plasma membrane H+-ATPase |
| title_full_unstemmed | Structure and activation mechanism of the hexameric plasma membrane H+-ATPase |
| title_short | Structure and activation mechanism of the hexameric plasma membrane H+-ATPase |
| title_sort | structure and activation mechanism of the hexameric plasma membrane h atpase |
| url | https://doi.org/10.1038/s41467-021-26782-y |
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