Literature DB >> 16880552

Preliminary characterization of (nucleoside-2'-O-)-methyltransferase crystals from Meaban and Yokose flaviviruses.

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.

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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


  10 in total

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  10 in total
  3 in total

1.  Structural bases for substrate recognition and activity in Meaban virus nucleoside-2'-O-methyltransferase.

Authors:  Eloise Mastrangelo; Michela Bollati; Mario Milani; Barbara Selisko; Frederic Peyrane; Bruno Canard; Gilda Grard; Xavier de Lamballerie; Martino Bolognesi
Journal:  Protein Sci       Date:  2007-05-01       Impact factor: 6.725

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  3 in total

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