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结核分枝杆菌DNA解旋酶ATP酶结构域的纯化、结晶及初步X射线晶体学研究

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

作者信息

Roué Mélanie, Agrawal Alka, Volker Craig, Mossakowska Danuta, Mayer Claudine, Bax Benjamin D

机构信息

Unité de Microbiologie Structurale, Institut Pasteur, CNRS UMR 3528, 25 rue du Dr Roux, 75015 Paris, France.

出版信息

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.

摘要

结核分枝杆菌DNA回旋酶是一种参与DNA拓扑结构调控的纳米机器,是该生物体中唯一存在的II型拓扑异构酶,因此是氟喹诺酮类药物治疗结核病的唯一靶点。ATP酶结构域通过ATP水解提供催化所需的能量。两种对应于这个43 kDa结构域的构建体,即Mtb-GyrB47(C1)和Mtb-GyrB47(C2),已被过量表达、纯化并结晶。从三种晶体形式收集了衍射数据。这些晶体属于空间群P1和P21,分别衍射到2.9 Å和3.3 Å的分辨率。

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