7ECD

Crystal structure of Tam41 from Firmicutes bacterium, complex with CTP-Mg

7ECD の概要

• エントリーDOI: 10.2210/pdb7ecd/pdb
• 分子名称: Phosphatidate cytidylyltransferase, CYTIDINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: cdp-dag synthase, phosphatidic acid, cytidine-diphosphate diacylglycerol, mitochondrial matrix, transferase
• 由来する生物種: Firmicutes bacterium CAG:884
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32714.87

構造登録者

Kimura, K.,Kawai, F.,Kubota-Kawai, H.,Watanabe, Y.,Tamura, Y. (登録日: 2021-03-12, 公開日: 2022-01-19, 最終更新日: 2024-05-29)

主引用文献

Kimura, K.,Kawai, F.,Kubota-Kawai, H.,Watanabe, Y.,Tomii, K.,Kojima, R.,Hirata, K.,Yamamori, Y.,Endo, T.,Tamura, Y.
Crystal structure of Tam41 cytidine diphosphate diacylglycerol synthase from a Firmicutes bacterium.
J.Biochem., 171:429-441, 2022

PubMed Abstract: 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.

PubMed: 34964897
DOI: 10.1093/jb/mvab154

実験手法

X-RAY DIFFRACTION (2.6 Å)