Caught in the Open

A Domain Insertion of M. tuberculosis Gyrase Suppresses ATPase Dimerization

Matthew J. Hobson, James M Berger

Research output: Contribution to journalShort survey

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.

Original languageEnglish (US)
Pages (from-to)561-563
Number of pages3
JournalStructure
Volume27
Issue number4
DOIs
StatePublished - Apr 2 2019

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Adenylyl Imidodiphosphate
Dimerization
Adenosine Triphosphatases
Tuberculosis
Enzymes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

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

In: Structure, Vol. 27, No. 4, 02.04.2019, p. 561-563.

Research output: Contribution to journalShort survey

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