Expression, purification, crystallization and preliminary X-ray studies of a prolyl-4-hydroxylase protein from Bacillus anthracis

被引：5
|
作者：
Miller, Megen A. [2 ]
Scott, Emily E. [1 ]
Limburg, Julian [2 ]
机构：
[1] Univ Kansas, Dept Med Chem, Lawrence, KS 66045 USA
[2] Univ Kansas, Dept Chem, Lawrence, KS 66045 USA
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷
基金：
美国国家卫生研究院;
关键词：
D O I：
10.1107/S1744309108023439
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Collagen prolyl-4-hydroxylase (C-P4H) catalyzes the hydroxylation of specific proline residues in procollagen, which is an essential step in collagen biosynthesis. A new form of P4H from Bacillus anthracis (anthrax-P4H) that shares many characteristics with the type I C-P4H from human has recently been characterized. The structure of anthrax-P4H could provide important insight into the chemistry of C-P4Hs and into the function of this unique homodimeric P4H. X-ray diffraction data of selenomethionine-labeled anthrax-P4H recombinantly-expressed in Escherichia coli have been collected to 1.4 angstrom resolution.
引用
收藏
页码：788 / 791
页数：4
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