The Nsp9 Replicase Protein of SARS-coronavirus, Structure and Functional Insights

Overview

Journal Structure

Publisher Cell Press

Specialties Biochemistry
Biotechnology
Cell Biology
Molecular Biology

Date 2004 Feb 14

PMID 14962394

Citations 154

Authors

Geoff Sutton

Elizabeth Fry

Lester Carter

Sarah Sainsbury

Tom Walter

Joanne Nettleship

Nick Berrow

Ray Owens

Robert Gilbert

Andrew Davidson

Stuart Siddell

Leo L M Poon

Jonathan Diprose

David Alderton

Martin Walsh

Jonathan M Grimes

David I Stuart

Affiliations

Soon will be listed here.

Abstract

As part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV) proteins, we have solved the structure of the non-structural protein 9 (nsp9). This protein, encoded by ORF1a, has no designated function but is most likely involved with viral RNA synthesis. The protein comprises a single beta-barrel with a fold previously unseen in single domain proteins. The fold superficially resembles an OB-fold with a C-terminal extension and is related to both of the two subdomains of the SARS-CoV 3C-like protease (which belongs to the serine protease superfamily). nsp9 has, presumably, evolved from a protease. The crystal structure suggests that the protein is dimeric. This is confirmed by analytical ultracentrifugation and dynamic light scattering. We show that nsp9 binds RNA and interacts with nsp8, activities that may be essential for its function(s).

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