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First published online February 25, 2005; 10.1104/pp.104.048751

Plant Physiology 137:1009-1017 (2005)
© 2005 American Society of Plant Biologists

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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Crystal Structures of Alfalfa Caffeoyl Coenzyme A 3-O-Methyltransferase1

Jean-Luc Ferrer, Chloe Zubieta2, Richard A. Dixon and Joseph P. Noel*

Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale, 38027 Grenoble cedex 1, France (J.-L.F.); Jack Skirball Chemical Biology and Proteomics Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037 (C.Z., J.P.N.); Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92037 (C.Z., J.P.N.); and Plant Biology Division, Samuel Roberts Noble Foundation, Ardmore, Oklahoma 73401 (R.A.D.)

Caffeoyl coenzyme A 3-O-methyltransferases (CCoAOMTs) are S-adenosyl-L-methionine-dependent O-methyltransferases (OMTs) involved in lignin biosynthesis. Plant CCoAOMTs belong to a distinct family of OMTs, more closely related to the mammalian catechol OMTs than to other plant OMTs. The crystal structure of alfalfa (Medicago sativa) CCoAOMT in complex with the reaction products S-adenosine-L-homocysteine and feruloyl/sinapoyl CoAs presented here belong to a structurally and mechanistically distinct family of plant small molecule OMTs. These structures provide a new understanding of the substrate preferences and the catalytic mechanism accompanying CCoAOMT-mediated O-methylation of CoA-linked phenylpropanoid substrates.

1 This work was supported by the National Science Foundation (grant no. 0236027 to J.P.N.).

2 Present address: European Molecular Biology Laboratory, 38042 Grenoble cedex 9, France.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.048751.

* Corresponding author; e-mail noel{at}salk.edu; fax 858–452–3683.

Received June 25, 2004; returned for revision December 24, 2004; accepted December 28, 2004.




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