天蓝色链霉菌硫氧还蛋白还原酶的结晶与衍射分析
Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor.
作者信息
Koháryová Michaela, Brynda Jiří, Rezáčová Pavlína, Kollárová Marta
机构信息
Faculty of Natural Sciences, Department of Biochemistry, Commenius University, Bratislava, Slovakia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt 8):917-21. doi: 10.1107/S1744309111021385. Epub 2011 Jul 20.
Thioredoxin reductases are homodimeric flavoenzymes that catalyze the transfer of electrons from NADPH to oxidized thioredoxin substrate. Bacterial thioredoxin reductases represent a promising target for the development of new antibiotics. Recombinant thioredoxin reductase TrxB from Streptomyces coelicolor was crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected from cryocooled crystals to 2.4 Å resolution using a synchrotron-radiation source. The crystals belonged to the primitive monoclinic space group P2(1), with unit-cell parameters a = 82.9, b = 60.6, c = 135.4 Å, α = γ = 90.0, β = 96.5°.
硫氧还蛋白还原酶是同二聚体黄素酶，催化电子从NADPH转移至氧化型硫氧还蛋白底物。细菌硫氧还蛋白还原酶是开发新型抗生素的一个有前景的靶点。采用悬滴气相扩散法使来自天蓝色链霉菌的重组硫氧还蛋白还原酶TrxB结晶。使用同步辐射源从冷冻晶体收集X射线衍射数据，分辨率达到2.4 Å。晶体属于原始单斜空间群P2(1)，晶胞参数为a = 82.9、b = 60.6、c = 135.4 Å，α = γ = 90.0，β = 96.5°。
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