2FAV: Crystal Structure of Sars Macro Domain in Complex With Adp- Ribose at 1.8 a Resolution

Citation:
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.
PDB ID: 2FAVDownload
MMDB ID: 42180
PDB Deposition Date: 2005/12/8
Updated in MMDB: 2012/11 
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 2FAV: monomeric; determined by author
Molecular Components in 2FAV
Label Count Molecule
Protein (1 molecule)
1
Replicase Polyprotein 1AB (Pp1ab) (Orf1ab)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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