Structural and functional insights into the unique CBS–CP12 fusion protein family in cyanobacteria
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- Claudia Hackenberg
- European Molecular Biology Laboratory (EMBL), Deutsches Elektronen-Synchrotron (DESY), 22607 Hamburg, Germany;
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- Johanna Hakanpää
- European Molecular Biology Laboratory (EMBL), Deutsches Elektronen-Synchrotron (DESY), 22607 Hamburg, Germany;
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- Fei Cai
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;
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- Svetlana Antonyuk
- Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, Liverpool L69 7ZX, United Kingdom;
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- Caroline Eigner
- European Molecular Biology Laboratory (EMBL), Deutsches Elektronen-Synchrotron (DESY), 22607 Hamburg, Germany;
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- Sven Meissner
- Department of Microbiology, Institute for Biochemistry and Biology, University of Potsdam, 14476 Potsdam-Golm, Germany;
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- Mikko Laitaoja
- Department of Chemistry, University of Eastern Finland, FI-80101 Joensuu, Finland;
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- Janne Jänis
- Department of Chemistry, University of Eastern Finland, FI-80101 Joensuu, Finland;
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- Cheryl A. Kerfeld
- Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720;
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- Elke Dittmann
- Department of Microbiology, Institute for Biochemistry and Biology, University of Potsdam, 14476 Potsdam-Golm, Germany;
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- Victor S. Lamzin
- European Molecular Biology Laboratory (EMBL), Deutsches Elektronen-Synchrotron (DESY), 22607 Hamburg, Germany;
抄録
<jats:title>Significance</jats:title> <jats:p>Carbon fixation is arguably one of the most important metabolic processes on Earth. Stand-alone CP12 proteins are major players in the regulation of this pathway in all oxygenic photosynthetic organisms, yet their intrinsic disorder has so far hampered the capturing of a principal part of their structure. Here we provide structural insights into CP12 by investigating an uncharacterized CP12 fusion protein, CBS–CP12, which is widespread among cyanobacteria, and reveal a unique hexameric structure. Our data further extend the existing knowledge of the regulation of photosynthesis and carbon fixation by the CP12 protein family, suggesting a more versatile role of this protein family in global redox regulation, predominantly in bloom-forming cyanobacteria that pose major threats in lakes and reservoirs.</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 115 (27), 7141-7146, 2018-06-18
Proceedings of the National Academy of Sciences
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詳細情報 詳細情報について
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- CRID
- 1360861295267033600
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- ISSN
- 10916490
- 00278424
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- データソース種別
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- Crossref