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Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion

Nature volume 354, pages 3743 (07 November 1991) | Download Citation

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Abstract

Sindbis virus consists of a nucleocapsid core surrounded by a lipid membrane through which penetrate 80 glycoprotein trimers. The structure of the core protein comprising the coat surrounding the genomic RNA has been determined. The poly-peptide fold from residue 114 to residue 264 is homologous to that of chymotrypsin-like serine proteinases with catalytic residues His 141, Asp 163 and Ser 215 of the core protein positioned as in other serine proteinases. The C-terminal tryp-tophan remains in the P1 substrate site subsequent to the autocatalytic cis cleavage of the capsid protein, thus rendering the proteinase inactive. Model building of the Sindbis core protein dimer shows that the nucleocapsid is likely to have T=4 quasisymmetry.

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Affiliations

  1. Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA

    • Hok-Kin Choi
    • , Liang Tong
    • , Wladek Minor
    • , Philippe Dumas
    •  & Michael G. Rossmann
  2. Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

    • Ulrike Boege
  3. Institut für Virologie, Justus-Liebig-Universität Giessen, Frankfurter Strasse 107, D-6300 Giessen, Germany

    • Gerd Wengler
  4. Present address: Laboratoire de Cristallographie Biologique, Institut de Biologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, 15 rue René Descartes, 67084 Strasbourg Cedex, France.

    • Philippe Dumas
  5. To whom correspondence should be addressed.

    • Michael G. Rossmann

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https://doi.org/10.1038/354037a0

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