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1vid

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(New page: 200px<br /><applet load="1vid" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vid, resolution 2.&Aring;" /> '''CATECHOL O-METHYLTRANS...)
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[[Image:1vid.gif|left|200px]]<br /><applet load="1vid" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1vid, resolution 2.&Aring;" />
 
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'''CATECHOL O-METHYLTRANSFERASE'''<br />
 
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==Overview==
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==CATECHOL O-METHYLTRANSFERASE==
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Catechol O-methyltransferase (COMT, EC 2.1.1.6) is important in the, central nervous system because it metabolizes catecholamine, neurotransmitters such as dopamine. The enzyme catalyses the transfer of, the methyl group from S-adenosyl-L-methionine (AdoMet) to one hydroxyl, group of catechols. COMT also inactivates catechol-type compounds such as, L-DOPA. With selective inhibitors of COMT in combination with L-DOPA, a, new principle has been realized in the therapy of Parkinson's disease., Here we solve the atomic structure of COMT to 2.0 A resolution, which, provides new insights into the mechanism of the methyl transfer reaction., The co-enzyme-binding domain is strikingly similar to that of an, AdoMet-dependent DNA methylase, indicating that all AdoMet methylases may, have a common structure.
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<StructureSection load='1vid' size='340' side='right'caption='[[1vid]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1vid]] is a 1 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=1VID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VID FirstGlance]. <br>
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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]] 2&#8491;</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=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=1vid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vid OCA], [https://pdbe.org/1vid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vid RCSB], [https://www.ebi.ac.uk/pdbsum/1vid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vid ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/1vid_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vid ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1VID is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG, SAM and DNC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VID OCA].
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*[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of catechol O-methyltransferase., Vidgren J, Svensson LA, Liljas A, Nature. 1994 Mar 24;368(6469):354-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8127373 8127373]
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[[Category: Large Structures]]
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[[Category: Catechol O-methyltransferase]]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Liljas A]]
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[[Category: Liljas, A.]]
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[[Category: Svensson LA]]
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[[Category: Svensson, L.A.]]
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[[Category: Vidgren J]]
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[[Category: Vidgren, J.]]
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[[Category: DNC]]
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[[Category: MG]]
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[[Category: SAM]]
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[[Category: methyltransferase]]
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[[Category: neurotransmitter degradation]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:52:52 2007''
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Current revision

CATECHOL O-METHYLTRANSFERASE

PDB ID 1vid

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