2FAV

Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution

Summary for 2FAV

• Entry DOI: 10.2210/pdb2fav/pdb
• Descriptor: Replicase polyprotein 1ab (pp1ab) (ORF1AB), ADENOSINE-5-DIPHOSPHORIBOSE (3 entities in total)
• Functional Keywords: protein-adp-ribose complex, structural genomics, structural proteomics in europe, marseilles structural genomics program @ afmb, msgp, viral protein
• Biological source: SARS coronavirus
• Cellular location: Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P59641
• Total number of polymer chains: 3
• Total formula weight: 59377.19

Authors

Egloff, M.P.,Malet, H.,Marseilles Structural Genomics Program @ AFMB (MSGP) (deposition date: 2005-12-08, release date: 2006-10-10, Last modification date: 2024-11-13)

Primary citation

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.
Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.
J.Virol., 80:8493-8502, 2006

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.

PubMed: 16912299
DOI: 10.1128/JVI.00713-06

Experimental method

X-RAY DIFFRACTION (1.8 Å)