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Synthesis, purification and crystallographic studies of the C‐terminal sterol carrier protein type 2 (SCP‐2) domain of human hydroxysteroid dehydrogenase‐like protein 2
Author(s) -
Cheng Zhong,
Li Yao,
Sui Chun,
Sun Xiaobo,
Xie Yong
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15008559
Subject(s) - dehydrogenase , subfamily , sterol , crystallography , hydroxysteroid dehydrogenase , chemistry , escherichia coli , biochemistry , enzyme , stereochemistry , biology , cholesterol , gene
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 Å resolution. The crystal belonged to the trigonal space group P 3 1 21 (or P 3 2 21), with unit‐cell parameters a = b = 70.4, c = 60.6 Å, α = β = 90, γ = 120°. Two protein molecules are present in the asymmetric unit, resulting in a Matthews coefficient of 2.16 Å 3 Da −1 and an approximate solvent content of 43%.