The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world
- 8 March 2004
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 101 (11) , 3792-3796
- https://doi.org/10.1073/pnas.0307877101
Abstract
The recently identified etiological agent of the severe acute respiratory syndrome (SARS) belongs to Coronaviridae (CoV), a family of viruses replicating by a poorly understood mechanism. Here, we report the crystal structure at 2.7-A resolution of nsp9, a hitherto uncharacterized subunit of the SARS-CoV replicative polyproteins. We show that SARS-CoV nsp9 is a single-stranded RNA-binding protein displaying a previously unreported, oligosaccharide/oligonucleotide fold-like fold. The presence of this type of protein has not been detected in the replicative complexes of RNA viruses, and its presence may reflect the unique and complex CoV viral replication/transcription machinery.Keywords
This publication has 43 references indexed in Scilit:
- SCOP: A structural classification of proteins database for the investigation of sequences and structuresPublished by Elsevier ,2006
- Unique and Conserved Features of Genome and Proteome of SARS-coronavirus, an Early Split-off From the Coronavirus Group 2 LineagePublished by Elsevier ,2003
- The Genome Sequence of the SARS-Associated CoronavirusScience, 2003
- Characterization of a Novel Coronavirus Associated with Severe Acute Respiratory SyndromeScience, 2003
- ESPript: analysis of multiple sequence alignments in PostScript.Bioinformatics, 1999
- SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic modelActa Crystallographica Section D-Biological Crystallography, 1999
- CATH – a hierarchic classification of protein domain structuresPublished by Elsevier ,1997
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994