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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
11:42

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

Published on: November 1, 2012

The 1.58 Å resolution structure of the DNA-binding domain of bacteriophage SF6 small terminase provides new hints on

Stefano Benini1, Maria Chechik, Miguel Ortiz Lombardía

  • 1Laboratory of Bioorganic Chemistry and Crystallography, Faculty of Science and Technology, Free University of Bolzano, Piazza Università 5, 39100 Bolzano, Italy. stefano.benini@unibz.it

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
|April 3, 2013
PubMed

Insights

The crystal structure of a key DNA-packaging protein (G1P) from bacteriophage SF6 was determined. This reveals how the terminase enzyme interacts with DNA to initiate packaging in phages and herpesviruses.

Area of Science:

  • Structural biology
  • Virology
  • Molecular biology

Background:

  • DNA packaging in tailed bacteriophages and herpesviruses relies on a viral terminase complex.
  • The terminase complex in Bacillus subtilis bacteriophages SF6 and SPP1 comprises two proteins: G1P and G2P.

Purpose of the Study:

  • To determine the crystal structure of the N-terminal DNA-binding domain of bacteriophage SF6's small terminase subunit, G1P.
  • To propose a model for G1P interaction with the DNA packaging-initiation site based on structural comparisons.

Main Methods:

  • X-ray crystallography was used to determine the 3D structure of the G1P N-terminal domain.
  • Comparative structural analysis was performed with other known DNA-binding proteins.

Main Results:

  • The crystal structure of the N-terminal DNA-binding domain of bacteriophage SF6 G1P was successfully resolved.
  • Structural similarities were identified between G1P and other DNA-binding proteins.

Conclusions:

  • The determined structure provides insights into the molecular mechanisms of viral DNA packaging.
  • A general model for G1P binding to the packaging-initiation site can be proposed, aiding future research on phage and herpesvirus DNA packaging.
Keywords:
DNA-binding domainsG1PSF6bacteriophagesterminasesviruses

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