Structural basis for specificity in the poxvirus topoisomerase

Mol Cell. 2006 Aug 4;23(3):343-54. doi: 10.1016/j.molcel.2006.06.015.

Abstract

Although smallpox has been eradicated from the human population, it is presently feared as a possible agent of bioterrorism. The smallpox virus codes for its own topoisomerase enzyme that differs from its cellular counterpart by requiring a specific DNA sequence for activation of catalysis. Here we present crystal structures of the smallpox virus topoisomerase enzyme bound both covalently and noncovalently to a specific DNA sequence. These structures reveal the basis for site-specific DNA recognition, and they explain how catalysis is likely activated by formation of a specific enzyme-DNA interface. Unexpectedly, the poxvirus enzyme uses a major groove binding alpha helix that is not present in the human enzyme to recognize part of the core recognition sequence and activate the enzyme for catalysis. The topoisomerase-DNA complex structures also provide a three-dimensional framework that may facilitate the rational design of therapeutic agents to treat poxvirus infections.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Antiviral Agents / chemistry
  • Antiviral Agents / pharmacology
  • Camptothecin / chemistry
  • Camptothecin / pharmacology
  • Catalysis
  • Catalytic Domain / genetics
  • Crystallography, X-Ray
  • DNA Topoisomerases, Type I / chemistry*
  • DNA Topoisomerases, Type I / genetics
  • DNA, Superhelical / chemistry
  • DNA, Superhelical / genetics
  • DNA, Superhelical / metabolism
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / pharmacology
  • Models, Molecular
  • Mutation / genetics
  • Mutation, Missense / genetics
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship
  • Topoisomerase I Inhibitors
  • Variola virus / enzymology*
  • Variola virus / genetics

Substances

  • Antiviral Agents
  • DNA, Superhelical
  • Enzyme Inhibitors
  • Recombinant Proteins
  • Topoisomerase I Inhibitors
  • DNA Topoisomerases, Type I
  • Camptothecin

Associated data

  • PDB/2H7F
  • PDB/2H7G