6IG2
Structure of mitochondrial CDP-DAG synthase Tam41 complexed with CTP, delta 74, F240A
Summary for 6IG2
| Entry DOI | 10.2210/pdb6ig2/pdb |
| Descriptor | Phosphatidate cytidylyltransferase, mitochondrial, CYTIDINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | mitochondrial inner membrane, cdp-diacylglycerol synthase, ntase fold, transferase |
| Biological source | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Total number of polymer chains | 4 |
| Total formula weight | 143910.03 |
| Authors | Jiao, H.Z.,Yin, Y.,Liu, Z.F. (deposition date: 2018-09-23, release date: 2019-07-10, Last modification date: 2023-11-22) |
| Primary citation | Jiao, H.,Yin, Y.,Liu, Z. Structures of the Mitochondrial CDP-DAG Synthase Tam41 Suggest a Potential Lipid Substrate Pathway from Membrane to the Active Site. Structure, 27:1258-, 2019 Cited by PubMed Abstract: In mitochondria, CDP-diacylglycerol (CDP-DAG) is a crucial precursor for cardiolipin biosynthesis. Mitochondrial CDP-DAG is synthesized by the translocator assembly and maintenance protein 41 (Tam41) through an elusive process. Here we show that Tam41 adopts sequential catalytic mechanism, and report crystal structures of the bulk N-terminal region of Tam41 from Schizosaccharomyces pombe in the apo and CTP-bound state. The structure reveals that Tam41 contains a nucleotidyltransferase (NTase) domain and a winged helix domain. CTP binds to an "L"-shaped pocket sandwiched between the two domains. Rearrangement of a loop region near the active site is essential for opening the CTP-binding pocket. Docking of phosphatidic acid/CDP-DAG in the structure suggests a lipid entry/exit pathway connected to the "L"-shaped pocket. The C-terminal region of SpTam41 contains a positively charged amphipathic helix crucial for membrane association and participates in binding phospholipids. These results provide detailed insights into the mechanism of CDP-DAG biosynthesis in mitochondria. PubMed: 31178220DOI: 10.1016/j.str.2019.04.017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.882 Å) |
Structure validation
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