Conformational switching by the scaffolding protein D directs the assembly of bacteriophage φX174

Marc C. Morais, Megan Fisher, Shuji Kanamaru, Laralynne Przybyla, John Burgner, Bentley A. Fane, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

The three-dimensional structure of bacteriophage φX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 Å by X-ray crystallography. The crystals belong to space group P41212 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the φX174 procapsid structure. Furthermore, application of the crystallographic 41 symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies.

Original languageEnglish (US)
Pages (from-to)991-997
Number of pages7
JournalMolecular cell
Volume15
Issue number6
DOIs
StatePublished - Sep 24 2004

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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