2fav
|
Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution
OverviewOverview
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.
About this StructureAbout this Structure
2FAV is a Single protein structure of sequence from Human sars coronavirus with APR as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains., Egloff MP, Malet H, Putics A, Heinonen M, Dutartre H, Frangeul A, Gruez A, Campanacci V, Cambillau C, Ziebuhr J, Ahola T, Canard B, J Virol. 2006 Sep;80(17):8493-502. PMID:16912299
Page seeded by OCA on Wed Nov 21 10:27:41 2007