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Caught in the Open: A Domain Insertion of M. tuberculosis Gyrase Suppresses ATPase Dimerization
Matthew J Hobson1, James M Berger1
1Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Abstract:
In this issue of Structure, Petrella et al. (2019) determine the structure of a catalytically competent construct of M. tuberculosis gyrase. Surprisingly, both apo and AMPPNP-bound structures capture a previously unknown enzyme state that is stabilized by a domain insertion unique to Corynebacteriales and appears to help regulate ATPase cycling.
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