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

被引:8
|
作者
Roue, Melanie [1 ,2 ]
Agrawal, Alka [3 ]
Volker, Craig [4 ]
Mossakowska, Danuta [3 ]
Mayer, Claudine [1 ,2 ]
Bax, Benjamin D. [3 ]
机构
[1] Inst Pasteur, CNRS UMR 3528, Unite Microbiol Struct, F-75015 Paris, France
[2] Univ Paris Diderot, Sorbonne Paris Cite, F-75051 Paris, France
[3] GlaxoSmithKline, Med Res Ctr, Platform Technol Sci, Stevenage SG1 2NY, Herts, England
[4] GlaxoSmithKline, Platform Technol Sci, Upper Providence, PA USA
基金
美国国家科学基金会;
关键词
TOPOISOMERASES; INHIBITION;
D O I
10.1107/S1744309113012906
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 P2(1) and diffracted to resolutions of 2.9 and 3.3 angstrom, respectively.
引用
收藏
页码:679 / 682
页数:4
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