Expression, crystallization and preliminary crystallographic study of octaprenyl pyrophosphate synthase from Helicobacter pylori.
Expression, crystallization and preliminary crystallographic study of octaprenyl pyrophosphate synthase from Helicobacter pylori.
复制标题
幽门螺杆菌八异戊二烯焦磷酸合酶的表达、结晶和初步晶体学研究。
DOI:
10.1107/s1744309110051511
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发表时间:
2011
期刊:
影响因子:
--
通讯作者:
Defeng Li
中科院分区:
文献类型:
--
作者:
Jinyong Zhang;Xiaoli Zhang;X. Mao;Q. Zou;Defeng Li
Octaprenyl pyrophosphate synthase (OPPs) is involved in the synthesis of the side chains of ubiquinone and menaquinone and catalyzes consecutive condensation reactions of farnesyl pyrophosphate with isopentenyl pyrophosphate to generate polyprenyl pyrophosphate and pyrophosphate. In order to investigate the roles played by OPPs in the metabolism of ubiquinone and menaquinone and the enzymatic mechanisms of these enzymes, analysis of the structure-function relationship of OPPs from Helicobacter pylori was initiated. The gene for OPPs was cloned, the protein was expressed, purified and crystallized and a diffraction data set was collected to 2.00 Å resolution. The crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 109.33, c = 103.41 Å.