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

Matthew J Hobson; James M Berger

doi:10.1016/j.str.2019.03.010

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

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

Authors

Matthew J Hobson¹, James M Berger²

Affiliations

¹ Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
² Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: jmberger@jhmi.edu.

PMID: 30943386
DOI: 10.1016/j.str.2019.03.010

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.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Adenosine Triphosphatases
DNA Gyrase
Dimerization
Humans
Mycobacterium tuberculosis*
Tuberculosis*

Substances

Adenosine Triphosphatases
DNA Gyrase

Abstract

Publication types

MeSH terms

Substances

Grants and funding