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Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.

ABSTRACT: This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. Nuclear magnetic resonance chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.

SUBMITTER: Serrano P 

PROVIDER: S-EPMC2168779 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature

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Nuclear magnetic resonance structure of the N-terminal domain of nonstructural protein 3 from the severe acute respiratory syndrome coronavirus.

Serrano Pedro P   Johnson Margaret A MA   Almeida Marcius S MS   Horst Reto R   Herrmann Torsten T   Joseph Jeremiah S JS   Neuman Benjamin W BW   Subramanian Vanitha V   Saikatendu Kumar S KS   Buchmeier Michael J MJ   Stevens Raymond C RC   Kuhn Peter P   Wüthrich Kurt K  

Journal of virology 20070829 21

This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four beta-strands and two alpha-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has n  ...[more]

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