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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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene> and <scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</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= [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]  
</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>
}}
<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>
</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.
== 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==
1VID 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: 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: DNC]]
[[Category: MG]]
[[Category: SAM]]
[[Category: methyltransferase]]
[[Category: neurotransmitter degradation]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:46:02 2008''

Latest revision as of 11:46, 14 February 2024

CATECHOL O-METHYLTRANSFERASECATECHOL O-METHYLTRANSFERASE

Structural highlights

1vid is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1vid, resolution 2.00Å

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