1vid: Difference between revisions

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-[[Image:1vid.gif|left|200px]]
- {{Structure
+==CATECHOL O-METHYLTRANSFERASE==
-|PDB= 1vid |SIZE=350|CAPTION= <scene name='initialview01'>1vid</scene>, resolution 2.&Aring;
+<StructureSection load='1vid' size='340' side='right'caption='[[1vid]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <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>
+<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>
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+</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>
-|GENE=
+<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>
-|DOMAIN=
+<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>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vid OCA], [http://www.ebi.ac.uk/pdbsum/1vid PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vid RCSB]</span>
+== 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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/1vid_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
-'''CATECHOL O-METHYLTRANSFERASE'''
+==See Also==
+*[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-VID is a [[Single protein]] structure of sequence from [http://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].
-==Reference==
-Crystal structure of catechol O-methyltransferase., Vidgren J, Svensson LA, Liljas A, Nature. 1994 Mar 24;368(6469):354-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8127373 8127373]
-[[Category: Catechol O-methyltransferase]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Liljas A]]
-[[Category: Liljas, A.]]
+[[Category: Svensson LA]]
-[[Category: Svensson, L A.]]
+[[Category: Vidgren J]]
-[[Category: Vidgren, J.]]
-[[Category: methyltransferase]]
-[[Category: neurotransmitter degradation]]
-[[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:53 2008''