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

Matthew J. Hobson, James M. Berger

School of Medicine

Research output: Contribution to journal › Short survey › peer-review

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 language	English (US)
Pages (from-to)	561-563
Number of pages	3
Journal	Structure
Volume	27
Issue number	4
DOIs	https://doi.org/10.1016/j.str.2019.03.010
State	Published - Apr 2 2019

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Access to Document

10.1016/j.str.2019.03.010

Cite this

@article{fa9e27c268174a3b9c0b8f809ea0ef92,

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

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.",

author = "Hobson, {Matthew J.} and Berger, {James M.}",

note = "Publisher Copyright: {\textcopyright} 2019 Elsevier Ltd",

year = "2019",

month = apr,

day = "2",

doi = "10.1016/j.str.2019.03.010",

language = "English (US)",

volume = "27",

pages = "561--563",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "4",

}

TY - JOUR

T1 - Caught in the Open

T2 - A Domain Insertion of M. tuberculosis Gyrase Suppresses ATPase Dimerization

AU - Hobson, Matthew J.

AU - Berger, James M.

PY - 2019/4/2

Y1 - 2019/4/2

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85063278640&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85063278640&partnerID=8YFLogxK

U2 - 10.1016/j.str.2019.03.010

DO - 10.1016/j.str.2019.03.010

M3 - Short survey

C2 - 30943386

AN - SCOPUS:85063278640

SN - 0969-2126

VL - 27

SP - 561

EP - 563

JO - Structure

JF - Structure

IS - 4

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this