Nomoto Ryohei, Tezuka Takeaki, Miyazono Ken-ichi, Tanokura Masaru, Horinouchi Sueharu, Ohnishi Yasuo
Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Tokyo 113-8657, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep 1;68(Pt 9):1085-8. doi: 10.1107/S1744309112030631. Epub 2012 Aug 31.
The mycobacterial integration host factor (mIHF) is a small nonspecific DNA-binding protein that is essential for the growth of Mycobacterium smegmatis. mIHF homologues are widely distributed among Actinobacteria, and a Streptomyces homologue of mIHF is involved in control of sporulation and antibiotic production in S. coelicolor A3(2). Despite their important biological functions, a structure of mIHF or its homologues has not been elucidated to date. Here, the S. griseus mIHF homologue (SGR6054) was expressed and purified from Escherichia coli and crystallized in the presence of a 16-mer duplex DNA by the sitting-drop vapour-diffusion method. The plate-shaped crystal belonged to space group C2, with unit-cell parameters a = 88.53, b = 69.35, c = 77.71 Å, β = 96.63°, and diffracted X-rays to 2.22 Å resolution.
分枝杆菌整合宿主因子（mIHF）是一种小的非特异性DNA结合蛋白，对耻垢分枝杆菌的生长至关重要。mIHF同源物广泛分布于放线菌中，mIHF的链霉菌同源物参与天蓝色链霉菌A3(2)的孢子形成和抗生素生产的控制。尽管它们具有重要的生物学功能，但迄今为止，mIHF或其同源物的结构尚未阐明。在这里，灰色链霉菌mIHF同源物（SGR6054）从大肠杆菌中表达并纯化，并通过坐滴气相扩散法在16聚体双链DNA存在下结晶。板状晶体属于空间群C2，晶胞参数a = 88.53，b = 69.35，c = 77.71 Å，β = 96.63°，X射线衍射分辨率为2.22 Å。
