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Crystal structure of the DNA-recognition component of the bacterial virus sf6 genome-packaging machine

Academic Article
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Overview

authors

  • Zhao, H. Y.
  • Finch, C. J.
  • Sequeira, R. D.
  • Johnson, B. A.
  • Johnson Jr., John
  • Casjens, S. R.
  • Tang, L.

publication date

  • February 2010

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • In herpesviruses and many bacterial viruses, genome-packaging is a precisely mediated process fulfilled by a virally encoded molecular machine called terminase that consists of two protein components: A DNA-recognition component that defines the specificity for packaged DNA, and a catalytic component that provides energy for the packaging reaction by hydrolyzing ATP. The terminase docks onto the portal protein complex embedded in a single vertex of a preformed viral protein shell called procapsid, and pumps the viral DNA into the procapsid through a conduit formed by the portal. Here we report the 1.65 A resolution structure of the DNA-recognition component gp1 of the Shigella bacteriophage Sf6 genome-packaging machine. The structure reveals a ring-like octamer formed by interweaved protein monomers with a highly extended fold, embracing a tunnel through which DNA may be translocated. The N-terminal DNA-binding domains form the peripheral appendages surrounding the octamer. The central domain contributes to oligomerization through interactions of bundled helices. The C-terminal domain forms a barrel with parallel beta-strands. The structure reveals a common scheme for oligomerization of terminase DNA-recognition components, and provides insights into the role of gp1 in formation of the packaging-competent terminase complex and assembly of the terminase with the portal, in which ring-like protein oligomers stack together to form a continuous channel for viral DNA translocation.

subject areas

  • Crystallography, X-Ray
  • DNA Packaging
  • DNA, Viral
  • Endodeoxyribonucleases
  • Genome, Viral
  • Macromolecular Substances
  • Microscopy, Electron, Transmission
  • Models, Molecular
  • Nucleic Acid Conformation
  • Podoviridae
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Shigella flexneri
  • Viral Proteins
  • Virus Assembly
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Research

keywords

  • DNA-packaging
  • bacteriophage
  • oligomer
  • protein:DNA interaction
  • terminase
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Identity

PubMed Central ID

  • PMC2836615

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0908569107

PubMed ID

  • 20133842
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Additional Document Info

start page

  • 1971

end page

  • 1976

volume

  • 107

issue

  • 5

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