A Human TOP2A Core DNA Binding X-ray Structure Reveals Topoisomerase Subunit Dynamics and a Potential Mechanism for SUMO Modulation of Decatenation

Abstract

In this issue of the Journal of Molecular Biology, Wendorff et al. describe the first structure of the active-site core of the human TOP2A protein in complex with DNA. This structure complements the X-ray model of the active core of the paralogous human protein TOP2B, which was published last year. Together, these two structures provide key information that will be relevant to understanding how these closely related proteins perform different roles during cell growth and tissue development. The new structure suggests a potential rationale to selectively target drugs to a single enzyme isotype and a functional role for SUMOylation.