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| | ==Arabidopsis thaliana phosphoethanolamine N-methyltransferase 1 (AtPMT1, XIOPTL) in complex with SAH and phosphocholine== | | ==Arabidopsis thaliana phosphoethanolamine N-methyltransferase 1 (AtPMT1, XIOPTL) in complex with SAH and phosphocholine== |
| - | <StructureSection load='5wp4' size='340' side='right' caption='[[5wp4]], [[Resolution|resolution]] 1.34Å' scene=''> | + | <StructureSection load='5wp4' size='340' side='right'caption='[[5wp4]], [[Resolution|resolution]] 1.34Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wp4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WP4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wp4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WP4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.341Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoethanolamine_N-methyltransferase Phosphoethanolamine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.103 2.1.1.103] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wp4 OCA], [http://pdbe.org/5wp4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wp4 RCSB], [http://www.ebi.ac.uk/pdbsum/5wp4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wp4 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5wp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wp4 OCA], [https://pdbe.org/5wp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wp4 RCSB], [https://www.ebi.ac.uk/pdbsum/5wp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wp4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEAM1_ARATH 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.<ref>PMID:15295103</ref> | + | [https://www.uniprot.org/uniprot/PEAM1_ARATH 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.<ref>PMID:15295103</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Phosphoethanolamine N-methyltransferase]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Jez, J M]] | + | [[Category: Large Structures]] |
| - | [[Category: Lee, S G]] | + | [[Category: Jez JM]] |
| - | [[Category: Atpmt1]] | + | [[Category: Lee SG]] |
| - | [[Category: Phosphoethanolamine n-methyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Xioptl]]
| + | |
| Structural highlights
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cruz-Ramirez A, Lopez-Bucio J, Ramirez-Pimentel G, Zurita-Silva A, Sanchez-Calderon L, Ramirez-Chavez E, Gonzalez-Ortega E, Herrera-Estrella L. The xipotl mutant of Arabidopsis reveals a critical role for phospholipid metabolism in root system development and epidermal cell integrity. Plant Cell. 2004 Aug;16(8):2020-34. PMID:15295103 doi:http://dx.doi.org/10.1105/tpc.103.018648
- ↑ Lee SG, Jez JM. Conformational changes in the di-domain structure of Arabidopsis phosphoethanolamine methyltransferase leads to active site formation. J Biol Chem. 2017 Oct 30. pii: jbc.RA117.000106. doi: 10.1074/jbc.RA117.000106. PMID:29084845 doi:http://dx.doi.org/10.1074/jbc.RA117.000106
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