3c3y

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(New page: 200px {{Structure |PDB= 3c3y |SIZE=350|CAPTION= <scene name='initialview01'>3c3y</scene>, resolution 1.371&Aring; |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+...)
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Revision as of 08:59, 2 April 2008


PDB ID 3c3y

Drag the structure with the mouse to rotate
, resolution 1.371Å
Sites: , , , and
Ligands: ,
Activity: Caffeoyl-CoA O-methyltransferase, with EC number 2.1.1.104
Domains: Methyltransf_3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of PFOMT, Phenylpropanoid and Flavonoid O-methyltransferase from M. crystallinum


Overview

Plant S-adenosyl-l-methionine-dependent class I natural product O-methyltransferases (OMTs), related to animal catechol OMTs, are dependent on bivalent cations and strictly specific for the meta position of aromatic vicinal dihydroxy groups. While the primary activity of these class I enzymes is methylation of caffeoyl coenzyme A OMTs, a distinct subset is able to methylate a wider range of substrates, characterized by the promiscuous phenylpropanoid and flavonoid OMT. The observed broad substrate specificity resides in two regions: the N-terminus and a variable insertion loop near the C-terminus, which displays the lowest degree of sequence conservation between the two subfamilies. Structural and biochemical data, based on site-directed mutagenesis and domain exchange between the two enzyme types, present evidence that only small topological changes among otherwise highly conserved 3-D structures are sufficient to differentiate between an enzymatic generalist and an enzymatic specialist in plant natural product methylation.

About this Structure

3C3Y is a Single protein structure of sequence from Mesembryanthemum crystallinum. Full crystallographic information is available from OCA.

Reference

Biochemical and Structural Analysis of Substrate Promiscuity in Plant Mg(2+)-Dependent O-Methyltransferases., Kopycki JG, Rauh D, Chumanevich AA, Neumann P, Vogt T, Stubbs MT, J Mol Biol. 2008 Feb 20;. PMID:18342334

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