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1 Department of Botany, University of Toronto, Toronto, Ontario M5S 3B2, Canada
2 Ontario Center for Structural Proteomics, University Health Network, Toronto, Ontario M5G 1L7, Canada
3 Structural Genomics Consortium and 4 Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario M5G 1L6, Canada
5 Midwest Center for Structural Genomics and Structural Biology, Argonne National Laboratory, Argonne, Illinois 60440, USA
(RECEIVED September 2, 2005; FINAL REVISION September 2, 2005; ACCEPTED September 7, 2005)
The S-adenosyl-L-methionine (SAM)-dependent methyltransferases represent a diverse and biologically important class of enzymes. These enzymes utilize the ubiquitous methyl donor SAM as a cofactor to methylate proteins, small molecules, lipids, and nucleic acids. Here we present the crystal structure of PH1915 from Pyrococcus horikoshii OT3, a predicted SAM-dependent methyltransferase. This protein belongs to the Cluster of Orthologous Group 1092, and the presented crystal structure is the first representative structure of this protein family. Based on sequence and 3D structure analysis, we have made valuable functional insights that will facilitate further studies for characterizing this group of proteins. Specifically, we propose that PH1915 and its orthologs are rRNA- or tRNA-specific methyltransferases.
Keywords: COG1092; crystal structure; methyltransferase; PH1915; S-adenosylmethionine
Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051821805.
Reprint requests to: Dinesh Christendat, Department of Botany, University of Toronto, 25 Willcocks Street, Toronto, Ontario M5S 3B2, Canada; e-mail: dinesh.christendat{at}utoronto.ca; fax: (416) 978-5878.
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