4ine: Difference between revisions

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New page: '''Unreleased structure''' The entry 4ine is ON HOLD Authors: Lukk, T., Nair, S.K. Description: Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed ...
 
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'''Unreleased structure'''


The entry 4ine is ON HOLD
==Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed with S-adenosyl homocysteine and phosphoethanolamine==
 
<StructureSection load='4ine' size='340' side='right'caption='[[4ine]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
Authors: Lukk, T., Nair, S.K.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4ine]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4INE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4INE FirstGlance]. <br>
Description: Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed with S-adenosyl homocysteine and phosphoethanolamine
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=OPE:PHOSPHORIC+ACID+MONO-(2-AMINO-ETHYL)+ESTER'>OPE</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'>[https://proteopedia.org/fgij/fg.htm?mol=4ine FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ine OCA], [https://pdbe.org/4ine PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ine RCSB], [https://www.ebi.ac.uk/pdbsum/4ine PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ine ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PMT2_CAEEL PMT2_CAEEL] Catalyzes the last two methylation reactions in the synthesis of phosphocholine, by converting phospho-monomethylethanolamine (N-methylethanolamine phosphate) into phospho-dimethylethanolamine (N,N-dimethylethanolamine phosphate) and the latter into phosphocholine. Phosphocholine is a precursor for phosphatidylcholine, a major component in membranes and a precursor itself in the production of glycoconjugates secreted by parasitic nematodes to avoid host immune responses.<ref>PMID:16681378</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Lukk T]]
[[Category: Nair SK]]

Latest revision as of 15:26, 20 September 2023

Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed with S-adenosyl homocysteine and phosphoethanolamine

4ine, resolution 1.45Å

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