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Crystal structure of reverse gyrase: insights into the positive supercoiling of DNA

By A.Chapin Rodríguez and Daniela Stock

Abstract

Reverse gyrase is the only topoisomerase known to positively supercoil DNA. The protein appears to be unique to hyperthermophiles, where its activity is believed to protect the genome from denaturation. The 120 kDa enzyme is the only member of the type I topoisomerase family that requires ATP, which is bound and hydrolysed by a helicase-like domain. We have determined the crystal structure of reverse gyrase from Archaeoglobus fulgidus in the presence and absence of nucleotide cofactor. The structure provides the first view of an intact supercoiling enzyme, explains mechanistic differences from other type I topoisomerases and suggests a model for how the two domains of the protein cooperate to positively supercoil DNA. Coordinates have been deposited in the Protein Data Bank under accession codes 1GKU and 1GL9

Topics: Article
Publisher: Oxford University Press
Year: 2002
DOI identifier: 10.1093/emboj
OAI identifier: oai:pubmedcentral.nih.gov:125824
Provided by: PubMed Central
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