1vid: Difference between revisions
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'''CATECHOL O-METHYLTRANSFERASE'''<br /> | '''CATECHOL O-METHYLTRANSFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
Catechol O-methyltransferase (COMT, EC 2.1.1.6) is important in the | 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. | ||
==About this Structure== | ==About this Structure== | ||
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:// | 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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SAM:'>SAM</scene> and <scene name='pdbligand=DNC:'>DNC</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1VID OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Liljas, A.]] | [[Category: Liljas, A.]] | ||
[[Category: Svensson, L | [[Category: Svensson, L A.]] | ||
[[Category: Vidgren, J.]] | [[Category: Vidgren, J.]] | ||
[[Category: DNC]] | [[Category: DNC]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:37 2008'' | ||
Revision as of 16:35, 21 February 2008
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CATECHOL O-METHYLTRANSFERASE
OverviewOverview
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.
About this StructureAbout this Structure
1VID is a Single protein structure of sequence from Rattus norvegicus with , and as ligands. Active as Catechol O-methyltransferase, with EC number 2.1.1.6 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of catechol O-methyltransferase., Vidgren J, Svensson LA, Liljas A, Nature. 1994 Mar 24;368(6469):354-8. PMID:8127373
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