Structure of a viral procapsid with molecular scaffolding

Terje Dokland, Robert McKenna, Leodevico L. Llag, Brian R. Bowman, Nino L. Incardona, Bentley A Fane, Michael G. Rossmann

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

The assembly of a macromolecular structure proceeds along an ordered morphogenetic pathway, and is accomplished by the switching of proteins between discrete conformations as they are added to the nascent assembly. Scaffolding proteins often play a catalytic role in the assembly process, rather like molecular chaperones. Although macromolecular assembly processes are fundamental to all biological systems, they have been characterized most thoroughly in viral systems, such as the icosahedral Escherichia coil bacteriophage ΦX174 (refs 6, 7). The ΦX174 virion contains the proteins F, G, H and J. During assembly, two scaffolding proteins B and D are required for the formation of a 108S, 360-Å-diameter procapsid from pentameric precursors containing the F, G and H protein. The procapsid contains 240 copies of protein D, forming an external scaffold, and 60 copies each of the internal scaffolding protein B, the capsid protein F, and the spike protein G. Maturation involves packaging of DNA and J proteins and loss of protein B, producing a 132S intermediate. Subsequent removal of the external scaffold yields the mature virion. Both the F and G proteins have the eight-stranded antiparallel β-sandwich motif common to many plant and animal viruses. Here we describe the structure of a procapsid-like particle at 3.5-Å resolution, showing how the scaffolding proteins coordinate assembly of the virus by interactions with the F and G proteins, and showing that the F protein undergoes conformational changes during capsid maturation.

Original languageEnglish (US)
Pages (from-to)308-313
Number of pages6
JournalNature
Volume389
Issue number6648
DOIs
StatePublished - 1997
Externally publishedYes

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Viral Structures
Proteins
GTP-Binding Proteins
Virion
DNA Packaging
Virus Assembly
Escherichia
Plant Viruses
Molecular Chaperones
Capsid
Capsid Proteins
Bacteriophages
Viruses

ASJC Scopus subject areas

  • General

Cite this

Dokland, T., McKenna, R., Llag, L. L., Bowman, B. R., Incardona, N. L., Fane, B. A., & Rossmann, M. G. (1997). Structure of a viral procapsid with molecular scaffolding. Nature, 389(6648), 308-313. https://doi.org/10.1038/38537

Structure of a viral procapsid with molecular scaffolding. / Dokland, Terje; McKenna, Robert; Llag, Leodevico L.; Bowman, Brian R.; Incardona, Nino L.; Fane, Bentley A; Rossmann, Michael G.

In: Nature, Vol. 389, No. 6648, 1997, p. 308-313.

Research output: Contribution to journalArticle

Dokland, T, McKenna, R, Llag, LL, Bowman, BR, Incardona, NL, Fane, BA & Rossmann, MG 1997, 'Structure of a viral procapsid with molecular scaffolding', Nature, vol. 389, no. 6648, pp. 308-313. https://doi.org/10.1038/38537
Dokland T, McKenna R, Llag LL, Bowman BR, Incardona NL, Fane BA et al. Structure of a viral procapsid with molecular scaffolding. Nature. 1997;389(6648):308-313. https://doi.org/10.1038/38537
Dokland, Terje ; McKenna, Robert ; Llag, Leodevico L. ; Bowman, Brian R. ; Incardona, Nino L. ; Fane, Bentley A ; Rossmann, Michael G. / Structure of a viral procapsid with molecular scaffolding. In: Nature. 1997 ; Vol. 389, No. 6648. pp. 308-313.
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