Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The crystal structure of a novel SAM-dependent methyltransferase PH1915 from Pyrococcus horikoshii.,Sun W, Xu X, Pavlova M, Edwards AM, Joachimiak A, Savchenko A, Christendat D Protein Sci. 2005 Dec;14(12):3121-8. Epub 2005 Oct 31. PMID:16260766[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sun W, Xu X, Pavlova M, Edwards AM, Joachimiak A, Savchenko A, Christendat D. The crystal structure of a novel SAM-dependent methyltransferase PH1915 from Pyrococcus horikoshii. Protein Sci. 2005 Dec;14(12):3121-8. Epub 2005 Oct 31. PMID:16260766 doi:10.1110/ps.051821805
