Preliminary characterization of (nucleoside-2′-O-)-methyltransferase crystals from Meaban and Yokose flaviviruses
- 24 July 2006
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section F Structural Biology and Crystallization Communications
- Vol. 62 (8), 768-770
- https://doi.org/10.1107/s1744309106025553
Abstract
Viral methyltranferases (MTase) are involved in the third step of the mRNA-capping process, transferring a methyl group from S-adenosyl-L-methionine (SAM) to the capped mRNA. MTases are classified into two groups: (guanine-N7)-methyltransferases (N7MTases), which add a methyl group onto the N7 atom of guanine, and (nucleoside-2'-O-)-methyltransferases (2'OMTases), which add a methyl group to a ribose hydroxyl. The MTases of two flaviviruses, Meaban and Yokose viruses, have been overexpressed, purified and crystallized in complex with SAM. Characterization of the crystals together with details of preliminary X-ray diffraction data collection (at 2.8 and 2.7 angstroms resolution, respectively) are reported here. The sequence homology relative to Dengue virus 2'OMTase and the structural conservation of specific residues in the putative active sites suggest that both enzymes belong to the 2'OMTase subgroup.Keywords
This publication has 10 references indexed in Scilit:
- The enzymes and control of eukaryotic mRNA turnoverNature Structural & Molecular Biology, 2004
- An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterizationThe EMBO Journal, 2002
- Use of TLS parameters to model anisotropic displacements in macromolecular refinementActa Crystallographica Section D-Biological Crystallography, 2001
- Structure, mechanism, and evolution of the mRNA capping apparatusProgress in Nucleic Acid Research and Molecular Biology, 2000
- Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl-GMP.Proceedings of the National Academy of Sciences, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assembliesStructure, 1994
- The NS 3 Nonstructural Protein of Flaviviruses Contains an RNA Triphosphatase ActivityVirology, 1993
- FLAVIVIRUS GENOME ORGANIZATION, EXPRESSION, AND REPLICATIONAnnual Review of Microbiology, 1990
- Solvent content of protein crystalsJournal of Molecular Biology, 1968