Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.

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

SUBMITTER: Egloff MP 

PROVIDER: S-EPMC1563857 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature