Crystallographic study of the iron-sulfur flavoprotein trimethylamine dehydrogenase from the bacterium W3A1.
Crystallographic study of the iron-sulfur flavoprotein trimethylamine dehydrogenase from the bacterium W3A1.
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来自细菌 W3A1 的铁硫黄素蛋白三甲胺脱氢酶的晶体学研究。
DOI：
10.1016/0022-2836(82)90551-4
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发表时间：
1982
影响因子：
5.6
通讯作者：
Steenkamp,DJ
中科院分区：
文献类型：
--
作者：
Lim,LW;Mathews,FS;Steenkamp,DJ
用宏晶种技术合成了同时含有[4Fe-4S]2+中心和共价结合的FMN的大单晶三甲胺脱氢酶。晶体属单斜晶系，空间群为P21，晶胞参数为a=147.63 Å，b=71.96 Å，c=83.66 Å，β=97.6 4°，衍射率至少达到2 o。每个不对称单位有一个大约166,000微米的二聚体。计算了一个5.0？分辨率的反常散射差分Patterson，它显示了非对称单元中两个[4Fe-4S]2+中心的存在和位置。在6.0？分辨率下计算的自转函数表示连接两个亚单位的非晶体2重轴。这些结果表明，三甲胺脱氢酶由两个相同或非常相似的亚基组成，每个亚基都含有一个[4Fe-4S]2+中心。
Large single crystals of trimethylamine dehydrogenase, containing both [4Fe-4S] 2+ centers and covalently bound FMN, have been prepared by the macro seeding technique. The crystals are monoclinic, space group P2 1 with cell parameters a= 147.63 A ̊, b= 71.96 A ̊, c= 83.66 A ̊ and β= 97.64°, and diffract to at least 2.0 Å resolution. There is one dimer of approximately 166,000 M m per asymmetric unit. A 5.0 Å resolution anomalous scattering difference Patterson has been computed which shows the presence and position of two [4Fe-4S] 2+ centers in the asymmetric unit. A self-rotation function computed at 6.0 Å resolution indicates a non-crystallographic 2-fold axis relating the two subunits. These results show trimethylamine dehydrogenase to be composed of two identical or very similar subunits each containing one [4Fe-4S] 2+ center.