Purification, crystallization and preliminary X-ray crystallographic studies of the Mycobacterium tuberculosis DNA gyrase ATPase domain

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):679-82. doi: 10.1107/S1744309113012906. Epub 2013 May 25.

Abstract

Mycobacterium tuberculosis DNA gyrase, a nanomachine involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and hence is the sole target of fluoroquinolones in the treatment of tuberculosis. The ATPase domain provides the energy required for catalysis by ATP hydrolysis. Two constructs corresponding to this 43 kDa domain, Mtb-GyrB47(C1) and Mtb-GyrB47(C2), have been overproduced, purified and crystallized. Diffraction data were collected from three crystal forms. The crystals belonged to space groups P1 and P21 and diffracted to resolutions of 2.9 and 3.3 Å, respectively.

Keywords: ATPase domain; DNA gyrase; Mycobacterium tuberculosis; type II topoisomerase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphatases / isolation & purification
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • DNA Gyrase / chemistry*
  • DNA Gyrase / isolation & purification
  • Mycobacterium tuberculosis / enzymology*

Substances

  • Bacterial Proteins
  • Adenosine Triphosphatases
  • DNA Gyrase