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Comment
. 2019 Apr 2;27(4):561-563.
doi: 10.1016/j.str.2019.03.010.

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

Matthew J Hobson  1 , James M Berger  2
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Caught in the Open: A Domain Insertion of M. tuberculosis Gyrase Suppresses ATPase Dimerization

Matthew J Hobson et al. Structure. .
Free article

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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