Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains
| Autor: | Christian Cambillau, John Ziebuhr, Marie-Pierre Egloff, Hélène Malet, Arnaud Gruez, Antoine Frangeul, Maarit Heinonen, Tero Ahola, Hélène Dutartre, Valérie Campanacci, Ákos Putics, Bruno Canard |
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| Přispěvatelé: | Architecture et fonction des Macromolécules Biologiques - UMR 6098 (AFMB), Centre National de la Recherche Scientifique (CNRS)-Université de Provence - Aix-Marseille 1, University of Würzburg, University of Helsinki, Centre for Cancer Research and Cell Biology, Queen's University [Belfast] (QUB), Architecture et fonction des macromolécules biologiques (AFMB), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Université de Provence - Aix-Marseille 1-Centre National de la Recherche Scientifique (CNRS), Helsingin yliopisto = Helsingfors universitet = University of Helsinki, Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Poly Adenosine Diphosphate Ribose Viral protein Poly ADP ribose polymerase viruses Immunology Molecular Sequence Data medicine.disease_cause Semliki Forest virus Microbiology Histones 03 medical and health sciences chemistry.chemical_compound Macro domain Structure-Activity Relationship Virology medicine Viral structural protein Hepatitis E virus Amino Acid Sequence health care economics and organizations 030304 developmental biology 0303 health sciences Adenosine Diphosphate Ribose Crystallography biology [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Adenosine diphosphate ribose 030302 biochemistry & molecular biology RNA biology.organism_classification Semliki forest virus 3. Good health Cell biology Chromatin Virus-Cell Interactions [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] stomatognathic diseases Biochemistry chemistry Severe acute respiratory syndrome-related coronavirus Insect Science [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology Poly(ADP-ribose) Polymerases |
| Zdroj: | Journal of Virology Journal of Virology, American Society for Microbiology, 2006, 80 (17), pp.8493-8502. ⟨10.1128/JVI.00713-06⟩ Journal of Virology, 2006, 80 (17), pp.8493-8502. ⟨10.1128/JVI.00713-06⟩ |
| ISSN: | 0022-538X 1098-5514 |
| DOI: | 10.1128/JVI.00713-06⟩ |
| Popis: | 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-Å 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. |
| Databáze: | OpenAIRE |
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