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エンドウ トシヤ
ENDO TOSHIYA
遠藤 斗志也 所属 京都産業大学 生命科学部 先端生命科学科 職種 客員教授 |
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| 発行・発表の年月 | 2021/12/29 |
| 形態種別 | 研究論文 |
| 標題 | Crystal structure of Tam41 cytidine diphosphate diacylglycerol synthase from a Firmicutes bacterium |
| 執筆形態 | その他 |
| 掲載誌名 | The Journal of Biochemistry |
| 出版社・発行元 | Oxford University Press (OUP) |
| 著者・共著者 | Keisuke Kimura,Fumihiro Kawai,Hisako Kubota-Kawai,Yasunori Watanabe,Kentaro Tomii,Rieko Kojima,Kunio Hirata,Yu Yamamori,Toshiya Endo,Yasushi Tamura |
| 概要 | <title>Abstract</title>
Translocator assembly and maintenance 41 (Tam41) catalyses the synthesis of cytidine diphosphate diacylglycerol (CDP-DAG), which is a high-energy intermediate phospholipid critical for generating cardiolipin in mitochondria. Although Tam41 is present almost exclusively in eukaryotic cells, a Firmicutes bacterium contains the gene encoding Tam41-type CDP-DAG synthase (FbTam41). FbTam41 converted phosphatidic acid (PA) to CDP-DAG using a ternary complex mechanism in vitro. Additionally, FbTam41 functionally substituted yeast Tam41 in vivo. These results demonstrate that Tam41-type CDP-DAG synthase functions in some prokaryotic cells. We determined the crystal structure of FbTam41 lacking the C-terminal 18 residues in the cytidine triphosphate (CTP)-Mg2+ bound form at a resolution of 2.6 Å. The crystal structure showed that FbTam41 contained a positively charged pocket that specifically accommodated CTP-Mg2+ and PA in close proximity. By using this structure, we constructed a model for the full-length structure of FbTam41 containing the last a-helix, which was missing in the crystal structure. Based on this model, we propose a molecular mechanism for CDP-DAG synthesis in bacterial cells and mitochondria. |
| DOI | 10.1093/jb/mvab154 |
| ISSN | 0021-924X/1756-2651 |
| PermalinkURL | https://academic.oup.com/jb/advance-article-pdf/doi/10.1093/jb/mvab154/42493522/mvab154.pdf |