嗜热栖热菌KOD1中[NiFe]-氢化酶成熟因子HypE的结晶及初步X射线晶体学研究
Crystallization and preliminary X-ray crystallographic study of [NiFe]-hydrogenase maturation factor HypE from Thermococcus kodakaraensis KOD1.
作者信息
Arai Takayuki, Watanabe Satoshi, Matsumi Rie, Atomi Haruyuki, Imanaka Tadayuki, Miki Kunio
机构信息
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):765-7. doi: 10.1107/S1744309107038833. Epub 2007 Aug 25.
The hydrogenase maturation protein HypE is involved in the biosynthesis of the CN ligands of the active-site iron of [NiFe] hydrogenases using carbamoylphosphate as a substrate. Here, the crystallization and preliminary crystallographic analysis of HypE from Thermococcus kodakaraensis KOD1 are reported. Crystals of HypE (338 amino acids, 35.9 kDa) have been obtained by the sitting-drop vapour-diffusion method using 2-methyl-2,4-pentanediol (MPD) as a precipitant. The crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 88.3, b = 45.8, c = 75.1 A. There is one HypE molecule in the asymmetric unit. A complete native X-ray diffraction data set was collected to a maximum resolution of 1.55 A at 100 K.
氢化酶成熟蛋白HypE利用氨基甲酰磷酸作为底物参与[NiFe]氢化酶活性位点铁的CN配体的生物合成。本文报道了来自嗜热栖热菌KOD1的HypE的结晶及初步晶体学分析。通过使用2-甲基-2,4-戊二醇（MPD）作为沉淀剂的坐滴气相扩散法获得了HypE（338个氨基酸，35.9 kDa）的晶体。这些晶体属于空间群P2(1)2(1)2，晶胞参数a = 88.3，b = 45.8，c = 75.1 Å。不对称单元中有一个HypE分子。在100 K下收集了完整的天然X射线衍射数据集，最大分辨率为1.55 Å。
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