Structural basis for membrane anchorage of viral phi29 DNA during replication

J Biol Chem. 2005 Dec 30;280(52):42486-8. doi: 10.1074/jbc.C500429200. Epub 2005 Nov 7.

Abstract

Prokaryotic DNA replication is compartmentalized at the cellular membrane. Functional and biochemical studies showed that the Bacillus subtilis phage 29-encoded membrane protein p16.7 is directly involved in the organization of membrane-associated viral DNA replication. The structure of the functional domain of p16.7 in complex with DNA, presented here, reveals the multimerization mode of the protein and provides insights in the organization of the phage genome at the membrane of the infected cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / metabolism
  • Bacillus subtilis / virology
  • Bacteriophages / metabolism*
  • Crystallography, X-Ray
  • DNA Replication
  • DNA, Viral / chemistry*
  • DNA, Viral / metabolism
  • Dimerization
  • Genome, Viral
  • Membrane Proteins / chemistry
  • Membrane Proteins / physiology*
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Viral Proteins / chemistry
  • Viral Proteins / physiology*

Substances

  • DNA, Viral
  • Membrane Proteins
  • Viral Proteins
  • protein p16.7, bacterophage phi29

Associated data

  • PDB/2C5R