Crystal Structure of Psb31, a Novel Extrinsic Protein of Photosystem II from a Marine Centric Diatom and Implications for Its Binding and Function
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- Ryo Nagao
- Department of Integrated Sciences in Physics and Biology, College of Humanities and Sciences, Nihon University, Sakurajosui 3-25-40, Setagaya-ku, Tokyo 156-8850, Japan
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- Michihiro Suga
- Graduate School of Natural Science and Technology/Faculty of Science, Okayama University, Tsushima Naka 3-1-1, Kita-ku, Okayama 700-8530, Japan
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- Ayako Niikura
- Graduate School of Natural Science and Technology/Faculty of Science, Okayama University, Tsushima Naka 3-1-1, Kita-ku, Okayama 700-8530, Japan
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- Akinori Okumura
- Department of Integrated Sciences in Physics and Biology, College of Humanities and Sciences, Nihon University, Sakurajosui 3-25-40, Setagaya-ku, Tokyo 156-8850, Japan
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- Faisal Hammad Mekky Koua
- Graduate School of Natural Science and Technology/Faculty of Science, Okayama University, Tsushima Naka 3-1-1, Kita-ku, Okayama 700-8530, Japan
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- Takehiro Suzuki
- Biomolecular Characterization Team, Discovery Research Institute, RIKEN, Hirosawa 2-1, Wako, Saitama 351-0198, Japan
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- Tatsuya Tomo
- Department of Biology, Faculty of Science, Tokyo University of Science, Kagurazaka 1-3, Shinjuku-ku, Tokyo 162-8601, Japan
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- Isao Enami
- Department of Biology, Faculty of Science, Tokyo University of Science, Kagurazaka 1-3, Shinjuku-ku, Tokyo 162-8601, Japan
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- Jian-Ren Shen
- Graduate School of Natural Science and Technology/Faculty of Science, Okayama University, Tsushima Naka 3-1-1, Kita-ku, Okayama 700-8530, Japan
説明
Psb31 is a fifth extrinsic protein found in photosystem II (PSII) of a centric diatom, Chaetoceros gracilis . The protein has been shown to bind directly to PSII in the absence of other extrinsic proteins and serves in part as a substitute for PsbO in supporting oxygen evolution. We report here the crystal structure of Psb31 at a resolution of 1.55 Å. The structure of Psb31 was composed of two domains, one major, N-terminal four helical domain and one minor, flexible C-terminal domain. The four helices in the N-terminal domain were arranged in an up-down-up-down fold, which appeared unexpectedly to be similar to the structure of spinach PsbQ, in spite of their low sequence homology. This suggests that the centric diatom PSII contains another PsbQ-type extrinsic protein in addition to the original PsbQ protein found in the organism. On the other hand, the C-terminal domain of Psb31 has a unique structure composed of one loop and one short helix. Based on these structural analysis and chemical cross-linking experiments, residues responsible for the binding of Psb31 to PSII intrinsic proteins were suggested. The results are discussed in relation to the copy number of extrinsic proteins in higher plant PSII.
収録刊行物
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- Biochemistry
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Biochemistry 52 (38), 6646-6652, 2013-09-11
American Chemical Society (ACS)
