3cbg
From Proteopedia
(New page: '''Unreleased structure''' The entry 3cbg is ON HOLD until Paper Publication Authors: Kopycki, J.G., Stubbs, M.T., Hagemann, M., Porzel, A., Schmidt, J., Schliemann, W., Zenk, M.H., Vog...) |
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| + | {{STRUCTURE_3cbg| PDB=3cbg | SCENE= }} | ||
| - | + | '''Functional and Structural Characterization of a Cationdependent O-Methyltransferase from the Cyanobacterium Synechocystis Sp. Strain PCC 6803''' | |
| - | Description: Functional and Structural Characterization of a Cationdependent O-Methyltransferase from the Cyanobacterium Synechocystis Sp. Strain PCC 6803 | ||
| + | ==Overview== | ||
| + | The coding sequence of the cyanobacterium Synechocystis sp. strain PCC 6803 slr0095 gene was cloned and functionally expressed in E. coli. The corresponding enzyme was classified as a cation- and S-adenosyl-L-methionine-dependent O-methyl-transferase (SynOMT), consistent with considerable amino acid sequence identities to eukaryotic O-methyltransferases (OMTs). The substrate specificity of SynOMT was similar with those of plant and mammalian CCoAOMT-like proteins accepting a variety of hydroxycinnamic acids and flavonoids as substrates. In contrast to the known mammalian and plant enzymes, which exclusively methylate the meta-hydroxyl position of aromatic di- and trihydroxy systems, SynOMT also methylates the para-position of hydroxycinnamic acids like 5-hydroxyferulic and 3,4,5-trihydroxy-cinnamic acid, resulting in the formation of novel compounds. The x-ray structure of SynOMT indicates that the active site allows for two alternative orientations of the hydroxylated substrates in comparison to the active sites of animal and plant enzymes, consistent with the observed preferred para-methylation and position promiscuity. Lys3 close to the N-terminus of the recombinant protein appears to play a key role in the activity of the enzyme. The possible implications of these results with respect to modifications of precursors of polymers like lignin are discussed. | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 | + | ==About this Structure== |
| + | 3CBG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CBG OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Functional and structural characterization of a cation-dependent O-methyltransferase from the cyanobacterium synechocystis SP. strain PCC 6803., Kopycki JG, Stubbs MT, Brandt W, Hagemann M, Porzel A, Schmidt J, Schliemann W, Zenk MH, Vogt T, J Biol Chem. 2008 May 23;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18502765 18502765] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Synechocystis sp.]] | ||
| + | [[Category: Kopycki, J G.]] | ||
| + | [[Category: Neumann, P.]] | ||
| + | [[Category: Stubbs, M T.]] | ||
| + | [[Category: Cyanobacterium]] | ||
| + | [[Category: O-methyltransferase]] | ||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 10:48:43 2008'' | ||
Revision as of 07:48, 11 June 2008
Functional and Structural Characterization of a Cationdependent O-Methyltransferase from the Cyanobacterium Synechocystis Sp. Strain PCC 6803
Overview
The coding sequence of the cyanobacterium Synechocystis sp. strain PCC 6803 slr0095 gene was cloned and functionally expressed in E. coli. The corresponding enzyme was classified as a cation- and S-adenosyl-L-methionine-dependent O-methyl-transferase (SynOMT), consistent with considerable amino acid sequence identities to eukaryotic O-methyltransferases (OMTs). The substrate specificity of SynOMT was similar with those of plant and mammalian CCoAOMT-like proteins accepting a variety of hydroxycinnamic acids and flavonoids as substrates. In contrast to the known mammalian and plant enzymes, which exclusively methylate the meta-hydroxyl position of aromatic di- and trihydroxy systems, SynOMT also methylates the para-position of hydroxycinnamic acids like 5-hydroxyferulic and 3,4,5-trihydroxy-cinnamic acid, resulting in the formation of novel compounds. The x-ray structure of SynOMT indicates that the active site allows for two alternative orientations of the hydroxylated substrates in comparison to the active sites of animal and plant enzymes, consistent with the observed preferred para-methylation and position promiscuity. Lys3 close to the N-terminus of the recombinant protein appears to play a key role in the activity of the enzyme. The possible implications of these results with respect to modifications of precursors of polymers like lignin are discussed.
About this Structure
3CBG is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
Functional and structural characterization of a cation-dependent O-methyltransferase from the cyanobacterium synechocystis SP. strain PCC 6803., Kopycki JG, Stubbs MT, Brandt W, Hagemann M, Porzel A, Schmidt J, Schliemann W, Zenk MH, Vogt T, J Biol Chem. 2008 May 23;. PMID:18502765 Page seeded by OCA on Wed Jun 11 10:48:43 2008
