Preliminary characterization of (nucleoside-2'-O-)-methyltransferase crystals from Meaban and Yokose flaviviruses
Mastrangelo, Eloise; Dalle, Karen; Bollati, Michela; Milani, Mario; Lantez, Violaine; de Lamballerie, Xavier; Brisbare, Nadege; Egloff, Marie-Pierre; Gould, Ernest; Coutard, Bruno; Canard, Bruno; Forrester, Naomi; Bolognesi, Martino. 2006 Preliminary characterization of (nucleoside-2'-O-)-methyltransferase crystals from Meaban and Yokose flaviviruses. Acta Crystallographica Section F, 62 (8). 768-770. https://doi.org/10.1107/S1744309106025553
Full text not available from this repository.Abstract/Summary
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 Å 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.
Item Type: | Publication - Article |
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Digital Object Identifier (DOI): | https://doi.org/10.1107/S1744309106025553 |
Programmes: | CEH Programmes pre-2009 publications > Biodiversity > BD03 The Genetic Basis of Ecological Function |
UKCEH and CEH Sections/Science Areas: | UKCEH Fellows Hails |
Additional Keywords: | (nucleoside-2'-O-)-methyltransferases, flaviviruses, Meaban virus, Yokose virus |
NORA Subject Terms: | Biology and Microbiology |
Date made live: | 15 Jan 2008 14:04 +0 (UTC) |
URI: | https://nora.nerc.ac.uk/id/eprint/2091 |
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