Crystallization and secondary-structure determination of a protein of the Lrp/AsnC family from a hyperthermophilic archaeon.
Crystallization and secondary-structure determination of a protein of the Lrp/AsnC family from a hyperthermophilic archaeon.
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来自超嗜热古菌的 Lrp/AsnC 家族蛋白的结晶和二级结构测定。
DOI：
10.1107/s0907444900020369
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
M. Suzuki
中科院分区：
文献类型：
--
作者：
N. Kudo;M. Allen;H. Koike;Y. Katsuya;M. Suzuki
从嗜热古细菌焦球菌（Pyrococcus sp. OT3）中分离得到Lrp/AsnC转录因子家族蛋白pot1216151。在大肠杆菌中，亮氨酸反应蛋白（leucine-responsive protein, Lrp）和AsnC调节许多代谢基因。po1216151晶体在传统x射线源下衍射到2.3 A，在同步辐射源下衍射到1.8 A。空间群为P3(1)21或P3(2)21，单元胞参数a = b = 96.9, c = 98.5 a。结合K(2)[Pt(CN)(6)]和K（AuCl(4)）衍生物的衍射数据，计算出分辨率为3.0 a的电子密度图。在不对称单元中鉴定了四个单体，每个单体具有四条-链和两条-螺旋。
A protein belonging to the Lrp/AsnC transcription-factor family, pot1216151, from the hyperthermophilic archaeon Pyrococcus sp. OT3 was crystallized. In Escherichia coli, leucine-responsive protein (Lrp) and AsnC regulate a number of metabolic genes. The crystals of pot1216151 diffracted to 2.3 A using a conventional X-ray source and to 1.8 A using a synchrotron-radiation source. The space group was identified to be P3(1)21 or P3(2)21, with unit-cell parameters a = b = 96.9, c = 98.5 A. In combination with diffraction data obtained from K(2)[Pt(CN)(6)] and K(AuCl(4)) derivatives, an electron-density map was calculated at a resolution of 3.0 A. Four monomers were identified in the asymmetric unit, with four beta-strands and two alpha-helices in each monomer.