@article{fdi:010046165,
  title = {{T}he crystal structures of {C}hikungunya and {V}enezuelan equine encephalitis virus ns{P}3 macro domains define a conserved adenosine binding pocket},
  author = {{M}alet, {H}. and {C}outard, {B}. and {J}amal, {S}. and {D}utartre, {H}. and {P}apageorgiou, {N}. and {N}euvonen, {M}. and {A}hola, {T}. and {F}orrester, {N}. and {G}ould, {E}. {A}. and {L}afitte, {D}. and {F}erron, {F}. and {L}escar, {J}. and {G}orbalenya, {A}. {E}. and de {L}amballerie, {X}avier and {C}anard, {B}.},
  editor = {},
  language = {{ENG}},
  abstract = {{M}acro domains (also called "{X} domains") constitute a protein module family present in all kingdoms of life, including viruses of the {C}oronaviridae and {T}ogaviridae families. {C}rystal structures of the macro domain from the {C}hikungunya virus (an "{O}ld {W}orld" alphavirus) and the {V}enezuelan equine encephalitis virus (a "{N}ew {W}orld" alphavirus) were determined at resolutions of 1.65 and 2.30 angstrom, respectively. {T}hese domains are active as adenosine di-phosphoribose 1 '-phosphate phosphatases. {B}oth the {C}hikungunya and the {V}enezuelan equine encephalitis virus macro domains are {ADP}-ribose binding modules, as revealed by structural and functional analysis. {A} single aspartic acid conserved through all macro domains is responsible for the specific binding of the adenine base. {S}equence-unspecific binding to long, negatively charged polymers such as poly({ADP}-ribose), {DNA}, and {RNA} is observed and attributed to positively charged patches outside of the active site pocket, as judged by mutagenesis and binding studies. {T}he crystal structure of the {C}hikungunya virus macro domain with an {RNA} trimer shows a binding mode utilizing the same adenine-binding pocket as {ADP}-ribose, but avoiding the {ADP}-ribose 1 '-phosphate phosphatase active site. {T}his leaves the {AMP} binding site as the sole common feature in all macro domains.},
  keywords = {},
  booktitle = {},
  journal = {{J}ournal of {V}irology},
  volume = {83},
  numero = {13},
  pages = {6534--6545},
  ISSN = {0022-538{X}},
  year = {2009},
  DOI = {10.1128/jvi.00189-09},
  URL = {https://www.documentation.ird.fr/hor/fdi:010046165},
}