Caught in the Open: A Domain Insertion of M. tuberculosis Gyrase Suppresses ATPase Dimerization

In this issue of Structure, Petrella et al. (2019) Petrella S. Capton E. Raynal B. Giffard C. Thureau A. Bonneté F. Alzari P.M. Aubry A. Mayer C. Overall structures of mycobacterium tuberculosis DNA gyrase reveal the role of a Corynebacteriales GyrB-specific insert in ATPase activity. Structure. 2019; 27 ( this issue) : 579-589 Google Scholar 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