@article{PAR00006536,
  title = {{C}rystal structure of a methyltransferase from a no-known-vector {F}lavivirus},
  author = {{B}ollati, {M}. and {M}ilani, {M}. and {M}astrangelo, {E}. and de {L}amballerie, {X}avier and {C}anard, {B}. and {B}olognes, {M}.},
  editor = {},
  language = {{ENG}},
  abstract = {{P}resently known flaviviruses belong to three major evolutionary branches: tick-borne viruses, mosquitoborne viruses and viruses with no known vector. {H}ere we present the crystal structure of the {Y}okose virus methyltransferase at 1.7 angstrom resolution, the first structure of a methyltransferase of a {F}lavivirus with no known vector. {S}tructural comparison of three methyltransferases representative of each of the {F}lavivirus branches shows that fold and structures are closely conserved, most differences being related to surface loops flexibility. {A}nalysis of the conserved residues throughout all the sequenced flaviviral methyltransferases reveals that, besides the central cleft hosting the substrate and cofactor binding sites, a second, almost continuous, patch is conserved and points away from active site towards the back of the protein. {T}he high level of structural conservation in this region could be functional for the methyl transferase/{RNA} interaction and stabilization of the ensuing complex.},
  keywords = {{F}lavivirus ; {RNA} capping ; {M}ethyltransferase ; {V}iral enzyme structure},
  booktitle = {},
  journal = {{B}iochemical and {B}iophysical {R}esearch {C}ommunications},
  volume = {382},
  numero = {1},
  pages = {200--204},
  ISSN = {0006-291{X}},
  year = {2009},
  DOI = {10.1016/j.bbrc.2009.03.008},
  URL = {https://www.documentation.ird.fr/hor/{PAR}00006536},
}