来自嗜热栖热菌的一种较大天然杂交蛋白的过氧化物还原酶结构域的过量生产、纯化、结晶及初步X射线分析。
Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein from Thermotoga maritima.
作者信息
Barbey Carole, Rouhier Nicolas, Haouz Ahmed, Navaza Alda, Jacquot Jean-Pierre
机构信息
Laboratoire de Biophysique Moléculaire, Cellulaire et Tissulaire, UMR 7033, Université Paris 13, UFR SMBH, 74 Rue Marcel Cachin, 93017 Bobigny Cedex, France.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jan 1;64(Pt 1):29-31. doi: 10.1107/S1744309107064391. Epub 2007 Dec 20.
Abstract
Thermotoga maritima contains a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus. The peroxiredoxin (Prx) domain has been overproduced and purified from Escherichia coli cells. The recombinant Prx domain, which is homologous to bacterial Prx BCP and plant Prx Q, folds properly into a stable protein that possesses biological activity. The recombinant protein was crystallized and synchrotron data were collected to 2.9 A resolution. The crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 176.67, c = 141.20 A.
摘要
嗜热栖热菌含有一种由两个部分组成的天然杂合蛋白
N端的过氧化物还原酶结构域和C端的硝基还原酶结构域。过氧化物还原酶（Prx）结构域已在大肠杆菌细胞中过量表达并纯化。与细菌Prx BCP和植物Prx Q同源的重组Prx结构域正确折叠成具有生物活性的稳定蛋白。该重组蛋白被结晶，并收集了分辨率为2.9 Å的同步辐射数据。晶体属于四方晶系空间群I422，晶胞参数a = b = 176.67，c = 141.20 Å。
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