2as0

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(New page: 200px<br /><applet load="2as0" size="350" color="white" frame="true" align="right" spinBox="true" caption="2as0, resolution 1.80&Aring;" /> '''Crystal Structure of...)
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Revision as of 16:08, 29 January 2008


2as0, resolution 1.80Å

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Crystal Structure of PH1915 (APC 5817): A Hypothetical RNA Methyltransferase

Overview

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.

About this Structure

2AS0 is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

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

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