Molecular mechanism underlying transport and allosteric inhibition of bicarbonate transporter SbtA
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- Sunzhenhe Fang
- National Key Laboratory of Plant Molecular Genetics, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China
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- Xiaowei Huang
- National Key Laboratory of Plant Molecular Genetics, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China
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- Xue Zhang
- National Key Laboratory of Plant Molecular Genetics, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China
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- Minhua Zhang
- National Key Laboratory of Plant Molecular Genetics, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China
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- Yahui Hao
- National Key Laboratory of Plant Molecular Genetics, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China
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- Hui Guo
- National Key Laboratory of Plant Molecular Genetics, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China
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- Lu-Ning Liu
- Institute of Systems, Molecular and Integrative Biology, University of Liverpool, L69 7ZB Liverpool, United Kingdom
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- Fang Yu
- Shanghai Key Laboratory of Plant Molecular Sciences, College of Life Sciences, Shanghai Normal University, Shanghai 200234, China
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- Peng Zhang
- National Key Laboratory of Plant Molecular Genetics, Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China
説明
<jats:title>Significance</jats:title> <jats:p> SbtA is a sodium-dependent, high-affinity bicarbonate transporter in the cyanobacterial CO <jats:sub>2</jats:sub> -concentrating mechanism (CCM). The transport activity of SbtA is regulated by SbtB, which is additionally influenced by adenyl nucleotides. We determined the three-dimensional structures of SbtA in complex with SbtB in two different conformations: A model summarizing the molecular mechanism of transport and allosteric inhibition of SbtA was established based on structural and biochemical data. The transport and regulatory mechanism revealed by our study represents a valuable case to investigate allosteric regulation of membrane transporters and, more importantly, will benefit plant photosynthesis improvement using the CCM system. </jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 118 (22), e2101632118-, 2021-05-24
Proceedings of the National Academy of Sciences
