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International Conference on SARS - one year after the (first) outbreak

08. - 11.05.2004, Lübeck

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Progress in the structural and functional characterization of the coronavirus replicase complex: Crystal structure of the SARS-CoV Nsp9

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  • Marie-Pierre Egloff - University of Marseille, Marseille, France
  • François Ferron - University of Marseille, Marseille, France
  • Valérie Campanacci - University of Marseille, Marseille, France
  • Sonia Longhi - University of Marseille, Marseille, France
  • Corinne Rancurel - University of Marseille, Marseille, France
  • Hélène Dutartre - University of Marseille, Marseille, France
  • Eric J. Snijder - Leiden University Medical Center, Leiden, The Netherlands
  • Alexander E. Gorbalenya - Leiden University Medical Center, Leiden, The Netherlands
  • Christian Cambillau - University of Marseille, Marseille, France
  • corresponding author presenting/speaker Bruno Canard - University of Marseille, Marseille, France

International Conference on SARS - one year after the (first) outbreak. Lübeck, 08.-11.05.2004. Düsseldorf, Köln: German Medical Science; 2004. Doc04sars11.01

Die elektronische Version dieses Artikels ist vollständig und ist verfügbar unter: http://www.egms.de/de/meetings/sars2004/04sars053.shtml

Veröffentlicht: 26. Mai 2004

© 2004 Egloff et al.
Dieser Artikel ist ein Open Access-Artikel und steht unter den Creative Commons Lizenzbedingungen (http://creativecommons.org/licenses/by-nc-nd/3.0/deed.de). Er darf vervielfältigt, verbreitet und öffentlich zugänglich gemacht werden, vorausgesetzt dass Autor und Quelle genannt werden.

Gliederung

Text

In 2003, the SARS crisis has dramatically shown the scarcity of biochemical and structural data available regarding Coronaviruses. It is however anticipated that these data will greatly help anti-coronavirus drug-design, as examplified by recent work on the main protease. We are using a structural genomics approach aimed at determining the crystal structures of all the proteins encoded by the SARS-CoV genome. Currently, 28 ORFs or sub-ORFs have been targeted, and 20 proteins are in crystallization. Among those, 8 different SARS-CoV proteins, and 1 H229E-CoV have been crystallized. Here we report the crystal structure at 2.8 Å resolution of Nsp9 (113 residues), a protein from the replicase complex. Based on the crystal structure, its function has now been elucidated and awaits connection to a biological role in RNA metabolism. The crystal structure revealed that Nsp9 is a dimeric protein mainly consisting of b-strands and displaying a previously unreported overall folding resembling an OB-fold. Its partial similarity with trypsin-like proteases suggests that Nsp9 may have evolved from a protease ancestor. However, biochemical experiments support a role of Nsp9 in RNA binding, as predicted by an RNA track on the surface of the protein and relatedness with single-stranded nucleic acid binding (SSB) proteins. As this type of protein is unique in the RNA virus world, it may have a role in several processes such as recombination and the regulation of SARS-CoV replication/transcription.