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4fgz

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==Crystal Structure of Phosphoethanolamine Methyltransferase from Plasmodium falciparum in Complex with Amodiaquine==
==Crystal Structure of Phosphoethanolamine Methyltransferase from Plasmodium falciparum in Complex with Amodiaquine==
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<StructureSection load='4fgz' size='340' side='right' caption='[[4fgz]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
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<StructureSection load='4fgz' size='340' side='right'caption='[[4fgz]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fgz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FGZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fgz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FGZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CQA:4-[(7-CHLOROQUINOLIN-4-YL)AMINO]-2-[(DIETHYLAMINO)METHYL]PHENOL'>CQA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.994&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5833 PLAFA])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CQA:4-[(7-CHLOROQUINOLIN-4-YL)AMINO]-2-[(DIETHYLAMINO)METHYL]PHENOL'>CQA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgz OCA], [https://pdbe.org/4fgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fgz RCSB], [https://www.ebi.ac.uk/pdbsum/4fgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgz ProSAT]</span></td></tr>
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<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=4fgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fgz OCA], [http://pdbe.org/4fgz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fgz RCSB], [http://www.ebi.ac.uk/pdbsum/4fgz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fgz ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q6T755_PLAFA Q6T755_PLAFA]
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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 2.0A 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.
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Crystal structure of phosphoethanolamine methyltransferase from Plasmodium falciparum in complex with amodiaquine.,Lee SG, Alpert TD, Jez JM Bioorg Med Chem Lett. 2012 Aug 1;22(15):4990-3. Epub 2012 Jun 17. PMID:22771008<ref>PMID:22771008</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4fgz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Phosphoethanolamine N-methyltransferase]]
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[[Category: Large Structures]]
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[[Category: Plafa]]
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[[Category: Plasmodium falciparum]]
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[[Category: Alpert, T D]]
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[[Category: Alpert TD]]
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[[Category: Jez, J M]]
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[[Category: Jez JM]]
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[[Category: Lee, S G]]
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[[Category: Lee SG]]
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[[Category: Methylation]]
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[[Category: Sam binding]]
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[[Category: Sam-dependent methyltransferase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Phosphoethanolamine Methyltransferase from Plasmodium falciparum in Complex with Amodiaquine

PDB ID 4fgz

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