大肠杆菌CyaY（人类铁调素的结构同源物）的结晶及初步X射线晶体学分析
Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CyaY, a structural homologue of human frataxin.
作者信息
Lee M G, Cho S J, Yang J K, Song H K, Suh S W
机构信息
Department of Chemistry, College of Natural Sciences, Division of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
出版信息
Acta Crystallogr D Biol Crystallogr. 2000 Jul;56(Pt 7):920-1. doi: 10.1107/s0907444900005916.
CyaY is a 106-residue protein from Escherichia coli. It shows amino-acid sequence similarity to human frataxin and a frataxin homologue in Saccharomyces cerevisiae, Yfh1p. The former is associated with the disease Friedreich ataxia and the latter plays a key role in iron homeostasis in mitochondria. CyaY has been overexpressed in soluble form in E. coli. The recombinant protein with a His(6) tag at its C-terminus has been crystallized at 296 K using polyethylene glycol (PEG) 4000 as a precipitant. Native diffraction data have been collected to 1.8 A using Cu Kalpha X-rays. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 44.66, c = 99.87 A, alpha = beta = 90.0, gamma = 120.0 degrees. The asymmetric unit contains one molecule of recombinant CyaY, with a corresponding V(m) of 2.13 A(3) Da(-1) and solvent content of 42.3%.
CyaY是一种来自大肠杆菌的由106个氨基酸残基组成的蛋白质。它与人类的frataxin以及酿酒酵母中的frataxin同源物Yfh1p在氨基酸序列上具有相似性。前者与弗里德赖希共济失调症有关，后者在线粒体铁稳态中起关键作用。CyaY已在大肠杆菌中以可溶形式过量表达。其C端带有His(6)标签的重组蛋白已在296 K下使用聚乙二醇（PEG）4000作为沉淀剂进行了结晶。使用Cu Kα X射线收集到了分辨率为1.8 Å的天然衍射数据。晶体属于三方晶系空间群P3(1)21（或P3(2)21），晶胞参数a = b = 44.66 Å，c = 99.87 Å，α = β = 90.0°，γ = 120.0°。不对称单元包含一个重组CyaY分子，相应的V(m)为2.13 ų Da⁻¹，溶剂含量为42.3%。
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