2AS0
Crystal Structure of PH1915 (APC 5817): A Hypothetical RNA Methyltransferase
Summary for 2AS0
Entry DOI | 10.2210/pdb2as0/pdb |
Descriptor | hypothetical protein PH1915 (2 entities in total) |
Functional Keywords | rna methyltransferase, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transferase |
Biological source | Pyrococcus horikoshii |
Total number of polymer chains | 2 |
Total formula weight | 90664.87 |
Authors | Sun, W.,Xu, X.,Pavlova, M.,Edwards, A.M.,Joachimiak, A.,Savchenko, A.,Christendat, D.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2005-08-22, release date: 2005-09-20, Last modification date: 2024-11-06) |
Primary citation | Sun, W.,Xu, X.,Pavlova, M.,Edwards, A.M.,Joachimiak, A.,Savchenko, A.,Christendat, D. The crystal structure of a novel SAM-dependent methyltransferase PH1915 from Pyrococcus horikoshii. Protein Sci., 14:3121-3128, 2005 Cited by PubMed Abstract: 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. PubMed: 16260766DOI: 10.1110/ps.051821805 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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