Bacteriophage φ29 scaffolding protein gp7 before and after prohead assembly

Marc C. Morais, Shuji Kanamarul, Mohammed O. Badasso, Jaya S. Koti, Barbara A.L. Owen, Cynthia T. McMurray, Dwight L. Anderson, Michael G. Rossmann

Research output: Contribution to journalArticle

82 Scopus citations

Abstract

Three-dimensional structures of the double-stranded DNA bacteriophage φ29 scaffolding protein (gp7) before and after prohead assembly have been determined at resolutions of 2.2 and 2.8 Å, respectively. Both structures are dimers that resemble arrows, with a four-helix bundle composing the arrowhead and a coiled coil forming the tail. The structural resemblance of gp7 to the yeast transcription factor GCN4 suggests a DNA-binding function that was confirmed by native gel electrophoresis. DNA binding to gp7 may have a role in mediating the structural transition from prohead to mature virus and scaffold release. A cryo-EM analysis indicates that gp7 is arranged inside the capsid as a series of concentric shells. The position of the higher density features in these shells correlates with the positions of hexamers in the equatorial region of the capsid, suggesting that gp7 may regulate formation of the prolate head through interactions with these hexamers.

Original languageEnglish (US)
Pages (from-to)572-576
Number of pages5
JournalNature Structural Biology
Volume10
Issue number7
DOIs
StatePublished - Jul 1 2003
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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    Morais, M. C., Kanamarul, S., Badasso, M. O., Koti, J. S., Owen, B. A. L., McMurray, C. T., Anderson, D. L., & Rossmann, M. G. (2003). Bacteriophage φ29 scaffolding protein gp7 before and after prohead assembly. Nature Structural Biology, 10(7), 572-576. https://doi.org/10.1038/nsb939