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

08:00 EDT 2nd April 2019 | BioPortfolio

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

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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This article was published in the following journal.

Name: Structure (London, England : 1993)
ISSN: 1878-4186
Pages: 561-563

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A bacterial DNA topoisomerase II that catalyzes ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. Gyrase binds to DNA as a heterotetramer consisting two A and two B subunits. In the presence of ATP, gyrase is able to convert relaxed circular DNA duplex into a superhelix. In the absence of ATP, supercoiled DNA is relaxed by DNA gyrase.

The dormant form of TUBERCULOSIS where the person shows no obvious symptoms and no sign of the causative agent (Mycobacterium tuberculosis) in the SPUTUM despite being positive for tuberculosis infection skin test.

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Pathological conditions of the CARDIOVASCULAR SYSTEM caused by infection of MYCOBACTERIUM TUBERCULOSIS. Tuberculosis involvement may include the HEART; the BLOOD VESSELS; or the PERICARDIUM.

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