Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump
The oxaloacetate decarboxylase sodium pump (OAD) is a unique primary-active transporter that utilizes the free energy derived from oxaloacetate decarboxylation for sodium transport across the cell membrane. It is composed of 3 subunits: the α subunit catalyzes carboxyl-transfer from oxaloacetate to...
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eLife Sciences Publications Ltd
2020-05-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/53853 |
| _version_ | 1811181011257524224 |
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| author | Xin Xu Huigang Shi Xiaowen Gong Pu Chen Ying Gao Xinzheng Zhang Song Xiang |
| author_facet | Xin Xu Huigang Shi Xiaowen Gong Pu Chen Ying Gao Xinzheng Zhang Song Xiang |
| author_sort | Xin Xu |
| collection | DOAJ |
| description | The oxaloacetate decarboxylase sodium pump (OAD) is a unique primary-active transporter that utilizes the free energy derived from oxaloacetate decarboxylation for sodium transport across the cell membrane. It is composed of 3 subunits: the α subunit catalyzes carboxyl-transfer from oxaloacetate to biotin, the membrane integrated β subunit catalyzes the subsequent carboxyl-biotin decarboxylation and the coupled sodium transport, the γ subunit interacts with the α and β subunits and stabilizes the OAD complex. We present here structure of the Salmonella typhimurium OAD βγ sub-complex. The structure revealed that the β and γ subunits form a β3γ3 hetero-hexamer with extensive interactions between the subunits and shed light on the OAD holo-enzyme assembly. Structure-guided functional studies provided insights into the sodium binding sites in the β subunit and the coupling between carboxyl-biotin decarboxylation and sodium transport by the OAD β subunit. |
| first_indexed | 2024-04-11T09:11:11Z |
| format | Article |
| id | doaj.art-10777bf77a7e4996a1f05122f3150894 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:11:11Z |
| publishDate | 2020-05-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-10777bf77a7e4996a1f05122f31508942022-12-22T04:32:29ZengeLife Sciences Publications LtdeLife2050-084X2020-05-01910.7554/eLife.53853Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pumpXin Xu0Huigang Shi1Xiaowen Gong2Pu Chen3Ying Gao4Xinzheng Zhang5Song Xiang6https://orcid.org/0000-0001-9314-4684Department of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Medical University, Tianjin, ChinaNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China; University of Chinese Academy of Sciences, Beijing, ChinaCAS Key Laboratory of Nutrition, Metabolism and Food safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, ChinaDepartment of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Medical University, Tianjin, ChinaCAS Key Laboratory of Nutrition, Metabolism and Food safety, Shanghai Institute of Nutrition and Health, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, ChinaNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China; University of Chinese Academy of Sciences, Beijing, ChinaDepartment of Biochemistry and Molecular Biology, Key Laboratory of Immune Microenvironment and Disease (Ministry of Education), Tianjin Medical University, Tianjin, ChinaThe oxaloacetate decarboxylase sodium pump (OAD) is a unique primary-active transporter that utilizes the free energy derived from oxaloacetate decarboxylation for sodium transport across the cell membrane. It is composed of 3 subunits: the α subunit catalyzes carboxyl-transfer from oxaloacetate to biotin, the membrane integrated β subunit catalyzes the subsequent carboxyl-biotin decarboxylation and the coupled sodium transport, the γ subunit interacts with the α and β subunits and stabilizes the OAD complex. We present here structure of the Salmonella typhimurium OAD βγ sub-complex. The structure revealed that the β and γ subunits form a β3γ3 hetero-hexamer with extensive interactions between the subunits and shed light on the OAD holo-enzyme assembly. Structure-guided functional studies provided insights into the sodium binding sites in the β subunit and the coupling between carboxyl-biotin decarboxylation and sodium transport by the OAD β subunit.https://elifesciences.org/articles/53853primary-active transporterbiotin-dependent decarboxylase sodium pumpcryo-EMSalmonella typhimurium |
| spellingShingle | Xin Xu Huigang Shi Xiaowen Gong Pu Chen Ying Gao Xinzheng Zhang Song Xiang Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump eLife primary-active transporter biotin-dependent decarboxylase sodium pump cryo-EM Salmonella typhimurium |
| title | Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump |
| title_full | Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump |
| title_fullStr | Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump |
| title_full_unstemmed | Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump |
| title_short | Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump |
| title_sort | structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump |
| topic | primary-active transporter biotin-dependent decarboxylase sodium pump cryo-EM Salmonella typhimurium |
| url | https://elifesciences.org/articles/53853 |
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