View source for 5fhr


==Crystal structure of Y200L mutant of Rat Catechol-O-Methyltransferase in complex with AdoMet and 3,5-dinitrocatechol==
<StructureSection load='5fhr' size='340' side='right'caption='[[5fhr]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fhr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FHR 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]] 1.63&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5fhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fhr OCA], [https://pdbe.org/5fhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fhr RCSB], [https://www.ebi.ac.uk/pdbsum/5fhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fhr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COMT_RAT COMT_RAT] Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Catechol-O-methyltransferase (COMT), an important therapeutic target in the treatment of Parkinson's disease, is also being developed for biocatalytic processes, including vanillin production, although lack of regioselectivity has precluded its more widespread application. By using structural and mechanistic information, regiocomplementary COMT variants were engineered that deliver either meta- or para-methylated catechols. X-ray crystallography further revealed how the active-site residues and quaternary structure govern regioselectivity. Finally, analogues of AdoMet are accepted by the regiocomplementary COMT mutants and can be used to prepare alkylated catechols, including ethyl vanillin.

Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase.,Law BJ, Bennett MR, Thompson ML, Levy C, Shepherd SA, Leys D, Micklefield J Angew Chem Int Ed Engl. 2016 Jan 21. doi: 10.1002/anie.201508287. PMID:26797714<ref>PMID:26797714</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fhr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Levy C]]