| Autor: |
Keisuke Kimura, Fumihiro Kawai, Hisako Kubota-Kawai, Yasunori Watanabe, Kentaro Tomii, Rieko Kojima, Kunio Hirata, Yu Yamamori, Toshiya Endo, Yasushi Tamura |
| Rok vydání: |
2021 |
| Předmět: |
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| Zdroj: |
Journal of biochemistry. 171(4) |
| ISSN: |
1756-2651 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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