4FGZ
Crystal Structure of Phosphoethanolamine Methyltransferase from Plasmodium falciparum in Complex with Amodiaquine
Summary for 4FGZ
| Entry DOI | 10.2210/pdb4fgz/pdb |
| Descriptor | Phosphoethanolamine N-methyltransferase, 4-[(7-CHLOROQUINOLIN-4-YL)AMINO]-2-[(DIETHYLAMINO)METHYL]PHENOL, S-ADENOSYL-L-HOMOCYSTEINE, ... (5 entities in total) |
| Functional Keywords | sam-dependent methyltransferase, sam binding, methylation, transferase |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 2 |
| Total formula weight | 64550.45 |
| Authors | Lee, S.G.,Alpert, T.D.,Jez, J.M. (deposition date: 2012-06-05, release date: 2012-07-25, Last modification date: 2024-02-28) |
| Primary citation | Lee, S.G.,Alpert, T.D.,Jez, J.M. Crystal structure of phosphoethanolamine methyltransferase from Plasmodium falciparum in complex with amodiaquine. Bioorg.Med.Chem.Lett., 22:4990-4993, 2012 Cited by PubMed Abstract: Phosphoethanolamine N-methyltransferase (PMT) is essential for phospholipid biogenesis in the malarial parasite Plasmodium falciparum. PfPMT catalyzes the triple methylation of phosphoethanolamine to produce phosphocholine, which is then used for phosphatidylcholine synthesis. Here we describe the 2.0Å resolution X-ray crystal structure of PfPMT in complex with amodiaquine. To better characterize inhibition of PfPMT by amodiaquine, we determined the IC(50) values of a series of aminoquinolines using a direct radiochemical assay. Both structural and functional analyses provide a possible approach for the development of new small molecule inhibitors of PfPMT. PubMed: 22771008DOI: 10.1016/j.bmcl.2012.06.032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.994 Å) |
Structure validation
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