View source for 4krh


==SeMet Haemonchus contortus Phosphoethanolamine N-methyltransferase 2 in complex with S-adenosyl-L-methionine==
<StructureSection load='4krh' size='340' side='right'caption='[[4krh]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4krh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemonchus_contortus Haemonchus contortus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KRH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KRH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=4krh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4krh OCA], [https://pdbe.org/4krh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4krh RCSB], [https://www.ebi.ac.uk/pdbsum/4krh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4krh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U5HK48_HAECO U5HK48_HAECO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phosphobase methylation pathway is the major route for supplying phosphocholine to phospholipid biosynthesis in plants, nematodes, and Plasmodium. In this pathway, phosphoethanolamine N-methyltransferase (PMT) catalyzes the sequential methylation of phosphoethanolamine to phosphocholine. In the PMT, one domain (MT1) catalyzes methylation of phosphoethanolamine to phosphomonomethylethanolamine and a second domain (MT2) completes the synthesis of phosphocholine. The X-ray crystal structures of the di-domain PMT from the parasitic nematode Haemonchus contortus (HcPMT1 and HcPMT2) reveal that the catalytic domains of these proteins are structurally distinct and allow for selective methylation of phosphobase substrates using different active site architectures. These structures also reveal changes leading to loss of function in the vestigial domains of the nematode PMT. Divergence of function in the two nematode PMTs provides two distinct antiparasitic inhibitor targets within the same essential metabolic pathway. The PMTs from nematodes, plants, and Plasmodium also highlight adaptable metabolic modularity in evolutionarily diverse organisms.

Evolution of Structure and Mechanistic Divergence in Di-Domain Methyltransferases from Nematode Phosphocholine Biosynthesis.,Lee SG, Jez JM Structure. 2013 Sep 4. pii: S0969-2126(13)00291-8. doi:, 10.1016/j.str.2013.07.023. PMID:24012478<ref>PMID:24012478</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4krh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Haemonchus contortus]]
[[Category: Large Structures]]
[[Category: Jez JM]]
[[Category: Lee SG]]