Skip to Main Content (Press Enter)

Logo CNR
  • ×
  • Home
  • People
  • Outputs
  • Organizations
  • Expertise & Skills

UNI-FIND
Logo CNR

|

UNI-FIND

cnr.it
  • ×
  • Home
  • People
  • Outputs
  • Organizations
  • Expertise & Skills
  1. Outputs

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

Academic Article
Publication Date:
2006
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 angstrom 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.
Iris type:
01.01 Articolo in rivista
Keywords:
NONSTRUCTURAL PROTEIN; LIGHT-SCATTERING; RNA
List of contributors:
Bollati, Michela; MILANI DE MAYO DE MARI, Mario; Mastrangelo, Eloise
Authors of the University:
BOLLATI MICHELA
MASTRANGELO ELOISE
MILANI DE MAYO DE MARI MARIO
Handle:
https://iris.cnr.it/handle/20.500.14243/450214
Published in:
ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS
Journal
  • Overview

Overview

URL

http://onlinelibrary.wiley.com/doi/10.1107/S1744309106025553/abstract
  • Use of cookies

Powered by VIVO | Designed by Cineca | 26.5.0.0 | Sorgente dati: PREPROD (Ribaltamento disabilitato)