Download MendeleyStructural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.
Egloff, M.P., Malet, H., Putics, A., Heinonen, M., Dutartre, H., Frangeul, A., Gruez, A., Campanacci, V., Cambillau, C., Ziebuhr, J., Ahola, T., Canard, B.(2006) J Virol 80: 8493-8502
- PubMed: 16912299
- DOI: https://doi.org/10.1128/JVI.00713-06
- Primary Citation of Related Structures:
2FAV - PubMed Abstract:
Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.
Organizational Affiliation:
Centre National de la Recherche Scientifique and Universit¨¦s d'Aix-Marseille I et II, UMR 6098, Architecture et Fonction des Macromol¨¦cules Biologiques, Ecole Sup¨¦rieure d'Ing¨¦nieurs de Luminy-Case 925, France.
