Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductase.
Preliminary X-ray diffraction analysis of YqjH from Escherichia coli: a putative cytoplasmic ferri-siderophore reductase.
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大肠杆菌 YqjH 的初步 X 射线衍射分析：一种推定的细胞质铁铁载体还原酶。
DOI：
10.1107/s174430910802352x
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
K. Watson
中科院分区：
文献类型：
--
作者：
V. Bamford;M. Armour;Sue A. Mitchell;M. Cartron;S. Andrews;K. Watson
YqjH is a cytoplasmic FAD-containing protein from Escherichia coli; based on homology to ViuB of Vibrio cholerae, it potentially acts as a ferri-siderophore reductase. This work describes its overexpression, purification, crystallization and structure solution at 3.0 A resolution. YqjH shares high sequence similarity with a number of known siderophore-interacting proteins and its structure was solved by molecular replacement using the siderophore-interacting protein from Shewanella putrefaciens as the search model. The YqjH structure resembles those of other members of the NAD(P)H:flavin oxidoreductase superfamily.
大肠杆菌铁肠杆菌素酯酶的过表达和纯化。
DOI：
--
发表时间：
1992
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Brickman,TJ;McIntosh,MA
通讯作者：
McIntosh,MA
影响因子：
15
作者：
Lin, H;Fiscchbach, MA;Walsh, CT
通讯作者：
Walsh, CT