Synthesis, purification and crystallographic studies of the C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2
Synthesis, purification and crystallographic studies of the C-terminal sterol carrier protein type 2 (SCP-2) domain of human hydroxysteroid dehydrogenase-like protein 2
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人羟基类固醇脱氢酶样蛋白 2 的 C 端甾醇载体蛋白 2 型 (SCP-2) 结构域的合成、纯化和晶体学研究
DOI：
10.1107/s2053230x15008559
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发表时间：
2015-07-01
影响因子：
0.9
通讯作者：
Xie, Yong
中科院分区：
文献类型：
--
作者：
Cheng, Zhong;Li, Yao;Xie, Yong
人羟基类固醇脱氢酶样蛋白2（Human hydroxysteroid degradase-like protein 2，HSDL 2）是氧化还原酶短链脱氢酶/还原酶（shortchain dehydrogenase/reductase，SDR）亚家族的成员，含有N端催化结构域和C端固醇载体蛋白2型（SCP-2）结构域。在本研究中，人的HSDL 2的C-末端SCP-2结构域，包括残基Lys 318-Arg 416，在大肠杆菌中产生，纯化和结晶。收集X射线衍射数据至2.10埃分辨率。晶体属于三方空间群P3（1）21（或P3（2）21），晶胞参数a = B = 70.4，c = 60.6埃，α = β = 90，γ = 120度。两个蛋白质分子存在于不对称单元中，导致马修斯系数为2.16埃（3）Da（-1），溶剂含量约为43%。
Human hydroxysteroid dehydrogenase-like protein 2 (HSDL2) is a member of the short-chain dehydrogenase/reductase (SDR) subfamily of oxidoreductases and contains an N-terminal catalytic domain and a C-termianl sterol carrier protein type 2 (SCP-2) domain. In this study, the C-terminal SCP-2 domain of human HSDL2, including residues Lys318-Arg416, was produced in Escherichia coli, purified and crystallized. X-ray diffraction data were collected to 2.10 angstrom resolution. The crystal belonged to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 70.4, c = 60.6 angstrom, alpha = beta = 90, gamma = 120 degrees. Two protein molecules are present in the asymmetric unit, resulting in a Matthews coefficient of 2.16 angstrom(3) Da(-1) and an approximate solvent content of 43%.