2h7f
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| , resolution 2.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | TOP1 (Variola virus) | ||||||
| Activity: | DNA topoisomerase, with EC number 5.99.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of variola topoisomerase covalently bound to DNA
OverviewOverview
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.
About this StructureAbout this Structure
2H7F is a Single protein structure of sequence from Variola virus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for specificity in the poxvirus topoisomerase., Perry K, Hwang Y, Bushman FD, Van Duyne GD, Mol Cell. 2006 Aug 4;23(3):343-54. PMID:16885024
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