3C3Y

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

Summary for 3C3Y

• Entry DOI: 10.2210/pdb3c3y/pdb
• Descriptor: O-methyltransferase, CALCIUM ION, S-ADENOSYL-L-HOMOCYSTEINE, ... (4 entities in total)
• Functional Keywords: plant secondary metabolism, o-methyltransferase, transferase
• Biological source: Mesembryanthemum crystallinum (common iceplant)
• Total number of polymer chains: 2
• Total formula weight: 54126.03

Authors

Kopycki, J.G.,Rauh, D.,Neumann, P.,Stubbs, M.T. (deposition date: 2008-01-29, release date: 2008-04-01, Last modification date: 2024-03-13)

Primary citation

Kopycki, J.G.,Rauh, D.,Chumanevich, A.A.,Neumann, P.,Vogt, T.,Stubbs, M.T.
Biochemical and Structural Analysis of Substrate Promiscuity in Plant Mg(2+)-Dependent O-Methyltransferases
J.Mol.Biol., 378:154-164, 2008

PubMed Abstract: 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.

PubMed: 18342334
DOI: 10.1016/j.jmb.2008.02.019

Experimental method

X-RAY DIFFRACTION (1.371 Å)