View source for 6gkz


==Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and SAH==
<StructureSection load='6gkz' size='340' side='right'caption='[[6gkz]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gkz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Coptis_japonica Coptis japonica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GKZ 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]] 2.43&#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=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=6gkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gkz OCA], [https://pdbe.org/6gkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gkz RCSB], [https://www.ebi.ac.uk/pdbsum/6gkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gkz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q948P7_COPJA Q948P7_COPJA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Benzylisoquinoline alkaloids (BIAs) are a structurally diverse family of plant secondary metabolites which have been exploited to develop analgesics, antibiotics, antitumor agents and other therapeutic agents. Biosynthesis of BIAs proceeds via a common pathway from tyrosine to (S)-reticulene at which point the pathway diverges. Coclaurine N-methyltransferase (CNMT) is a key enzyme in the pathway to (S)-reticulene, installing the N-methyl substituent that is essential for the bioactivity of many BIAs. In this paper, we describe the first crystal structure of CNMT which, along with mutagenesis studies, defines the enzymes active site architecture. The specificity of CNMT was also explored with a range of natural and synthetic substrates as well as co-factor analogues. Knowledge from this study could be used to generate improved CNMT variants required to produce BIAs or synthetic derivatives.

Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase.,Bennett M, Thompson M, Shepherd S, Dunstan M, Herbert A, Smith D, Cronin V, Menon B, Levy C, Micklefield J Angew Chem Int Ed Engl. 2018 May 23. doi: 10.1002/anie.201805060. PMID:29791083<ref>PMID:29791083</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6gkz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Coptis japonica]]
[[Category: Large Structures]]
[[Category: Dunstan MS]]
[[Category: Levy CW]]