Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase crystals from Thermotoga maritima and Escherichia coli

被引：6

作者：

Guo, RT

Ko, TP

Chou, CC

Shr, HL

Chu, HM

Tsai, YH

Liang, PH

Wang, AHJ ^{[1
]}

机构：

[1] Acad Sinica, Taiwan Int Grad Program, Taipei 115, Taiwan

[2] Natl Taiwan Univ, Inst Biochem Sci, Taipei 106, Taiwan

[3] Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan

[4] Acad Sinica, Core Facil Protein Xray Crystallog, Taipei 115, Taiwan

[5] Natl Yang Ming Univ, Inst Biochem, Taipei 112, Taiwan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903018985

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Octaprenyl pyrophosphate synthase (OPPs) catalyzes the condensation of five isopentenyl pyrophosphates with farnesyl pyrophosphate to generate C-40 octaprenyl pyrophosphate. The enzymes from the hyperthermophilic bacterium Thermotoga maritima and from the mesophilic Escherichia coli were expressed in E. coli and the recombinant proteins were purified and crystallized. The T. maritima OPPs crystals belong to space group P42(1)2, with unit-cell parameters a = b = 151.53, c = 69.72 Angstrom. The E. coli OPPs crystals belong to space group C222(1), with unit-cell parameters a = 247.66, b = 266.10, c = 157.93 Angstrom. Diffraction data were collected at 100 K using synchrotron radiation and an in-house X-ray source. Structure determination of T. maritima OPPs has been carried out using MIR data sets at 2.8 Angstrom resolution. The asymmetric unit contains one dimer. An initial model with 280 residues per subunit has been built and refined to 2.28 Angstrom resolution. It shows mostly helical structure and resembles that of avian farnesyl pyrophosphate synthase.

引用

页码：2265 / 2268

页数：4

共 22 条

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