| Literature DB >> 16880552 |
Eloise Mastrangelo1, Michela Bollati, Mario Milani, Xavier de Lamballerie, Xavier de Lamballeire, Nadège Brisbarre, Nadege Brisbare, Karen Dalle, Violaine Lantez, Marie Pierre Egloff, Bruno Coutard, Bruno Canard, Ernest Gould, Naomi Forrester, Martino Bolognesi.
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.Entities:
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Year: 2006 PMID: 16880552 PMCID: PMC2242907 DOI: 10.1107/S1744309106025553
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091