%0 Journal Article
%T Caught in the Open: A Domain Insertion of M. tuberculosis Gyrase Suppresses ATPase Dimerization
%J -
%D 2019
%R https://doi.org/10.1016/j.str.2019.03.010
%X In this issue of Structure, Petrella et al. (2019) Petrella S. Capton E. Raynal B. Giffard C. Thureau A. Bonnet¨¦ 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
%U https://www.cell.com/structure/fulltext/S0969-2126(19)30088-7