Purification, crystallisation and preliminary crystallographic studies of succinate:ubiquinone oxidoreductase from Escherichia coli.

Purification, crystallisation and preliminary crystallographic studies of succinate:ubiquinone oxidoreductase from Escherichia coli.
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大肠杆菌琥珀酸:泛醌氧化还原酶的纯化、结晶和初步晶体学研究。

DOI:
10.1016/s0005-2728(01)00236-5
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发表时间:
2002
期刊:
Biochimica et biophysica acta
影响因子:
--
通讯作者:
Iwata,So
Iwata,So
中科院分区:
--
文献类型:
--
作者:
Törnroth,Susanna;Yankovskaya,Victoria;Cecchini,Gary;Iwata,So

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从大肠杆菌中分离纯化了一种膜蛋白复合物琥珀酸脱氢酶(SQR)。该酶由含有FAD的四个亚基、三个铁硫簇和一个作为辅基的血红素B组成。晶体属六方晶系,空间群P63,晶胞参数a=B=123.8,c=214.6。晶体的不对称单元含有一个SQR单体(Mr 120 kDa)。现在,数据集的分辨率为4.0 nm,完整性为88.1%,Rmerge为0.106。利用E. coli QFR(延胡索酸还原酶)作为搜索模型。包装表明E. coliSQR是晶体学上的三聚体,而不是像在E. coli QFR。
A membrane protein complex, succinate dehydrogenase (SQR) from Escherichia coli has been purified and crystallised. This enzyme is composed of four subunits containing FAD, three iron–sulphur clusters and one haem b as prosthetic groups. The obtained crystals belong to the hexagonal space group P63with the unit-cell dimensions of a=b=123.8 Å and c=214.6 Å. An asymmetric unit of the crystals contains one SQR monomer (Mr120 kDa). A data set is now available at 4.0 Å resolution with 88.1% completeness and 0.106 Rmerge. We have obtained a molecular replacement solution that shows sensible molecular packing, using the soluble domain of E. coli QFR (fumarate reductase) as a search model. The packing suggests that E. coli SQR is a crystallographic trimer rather than a dimer as observed for the E. coli QFR.
DOI: 10.1006/prep.2000.1238
发表时间: 2000
期刊: Protein expression and purification.
影响因子: --
作者:
Luna-Chavez,C;Iverson,TM;Rees,DC;Cecchini,G
通讯作者: Cecchini,G
DOI: --
发表时间: 1993
期刊: The Journal of biological chemistry
影响因子: --
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影响因子: 3.5
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