5wp4 | pdb_00005wp4

Arabidopsis thaliana phosphoethanolamine N-methyltransferase 1 (AtPMT1, XIOPTL) in complex with SAH and phosphocholine

spinqualitylabelsall models 5wp4, resolution 1.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wp4 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PC, SAH Activity: Phosphoethanolamine N-methyltransferase, with EC number 2.1.1.103 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PEAM1_ARATH] Catalyzes N-methylation of phosphoethanolamine, phosphomonomethylethanolamine and phosphodimethylethanolamine, the three methylation steps required to convert phosphoethanolamine to phosphocholine. Required for root system development and epidermal cell integrity through its role in choline and phospholipid metabolism. Publication Abstract from PubMed Phosphocholine (pCho) is a precursor for phosphatidylcholine and osmoprotectants in plants. In plants, de novo synthesis of pCho relies on the phosphobase methylation pathway. Phosphoethanolamine methyltransferase (PMT) catalyzes the triple methylation of phosphoethanolamine (pEA) to pCho. The plant PMT are di-domain methyltransferases that divide the methylation of pEA in one domain from subsequent methylations in the second domain. To understand the molecular basis of this architecture, we examined the biochemical properties of three Arabidopsis thaliana PMT (AtPMT1-3) and determined the x-ray crystal structures of AtPMT1 and AtPMT2. Although each isoform synthesizes pCho from pEA, their physiological roles differ with AtPMT1 essential for normal growth and salt tolerance, whereas AtPMT2 and AtPMT3 overlap functionally. The structures of AtPMT1 and AtPMT2 reveal unique features in each methyltransferase domain, including active sites that use different chemical mechanisms for phosphobase methylation. These structures also show how rearrangements in the both active sites and the di-domain linker form catalytically competent active sites and provide insight on the evolution of the PMT in plants, nematodes, and apicomplexans. Connecting conformational changes with catalysis in modular enzymes, like the PMT, provides new insights on interdomain communication in biosynthetic systems. Conformational changes in the di-domain structure of Arabidopsis phosphoethanolamine methyltransferase leads to active site formation.,Lee SG, Jez JM J Biol Chem. 2017 Oct 30. pii: jbc.RA117.000106. doi: 10.1074/jbc.RA117.000106. PMID:29084845 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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