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NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH6.5

  • Margaret A. Johnson*
  • , Kristaps Jaudzems
  • , Kurt Wüthrich
  • *Corresponding author for this work
  • Scripps Research Institute

Research output: Contribution to journal › Article › peer-review

27 Citations (Scopus)

Abstract

The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.

Original languageEnglish
Pages (from-to)619-628
Number of pages10
JournalJournal of Molecular Biology
Volume402
Issue number4
DOIs
Publication statusPublished - Oct 2010
Externally publishedYes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

  • Conformational polymorphism
  • Coronavirus
  • NMR structure
  • Nsp7
  • Severe acute respiratory syndrome

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