@article{fdi:010052867,
  title = {{T}he 2{C} putative helicase of echovirus 30 adopts a hexameric ring-shaped structure},
  author = {{P}apageorgiou, {N}. and {C}outard, {B}. and {L}antez, {V}. and {G}autron, {E}. and {C}hauvet, {O}. and {B}aronti, {C}{\'e}cile and {N}order, {H}. and de {L}amballerie, {X}avier and {H}eresanu, {V}. and {F}erte, {N}. and {V}eesler, {S}. and {G}orbalenya, {A}. {E}. and {C}anard, {B}.},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he 2{C} protein, which is an essential {ATP}ase and one of the most conserved proteins across the {P}icornaviridae family, is an emerging antiviral target for which structural and functional characterization remain elusive. {B}ased on a distant relationship to helicases of small {DNA} viruses, piconavirus 2{C} proteins have been predicted to unwind double-stranded {RNA}s. {H}ere, a terminally extended variant of the 2{C} protein from echovirus 30 has been studied by means of enzymatic activity assays, transmission electron microscopy, atomic force microscopy and dynamic light scattering. {T}he transmission electron-microscopy technique showed the existence of ring-shaped particles with similar to 12 nm external diameter. {I}mage analysis revealed that these particles were hexameric and resembled those formed by superfamily 3 {DNA} virus helicases.},
  keywords = {2{C} protein ; echovirus 30 ; transmission electron microscopy},
  booktitle = {},
  journal = {{A}cta {C}rystallographica {S}ection {D}. {B}iological {C}rystallography},
  volume = {66},
  numero = {{P}art 10},
  pages = {1116--1120},
  ISSN = {0907-4449},
  year = {2010},
  DOI = {10.1107/s090744491002809x},
  URL = {https://www.documentation.ird.fr/hor/fdi:010052867},
}