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

Rey Ting Guo, Tzu Ping Ko, Chia Cheng Chou, Hui Lin Shr, Hsing Mao Chu, Yao Hsien Tsai, Po Huang Liang, Andrew H.J. Wang

研究成果: 雜誌貢獻文章同行評審

6 引文 斯高帕斯(Scopus)

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 12, with unit-cell parameters a = b = 151.53, c = 69.72 Å. The E. coli OPPs crystals belong to space group C2221, with unit-cell parameters a = 247.66, b = 266.10, c = 157.93 Å. 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 Å resolution. The asymmetric unit contains one dimer. An initial model with 280 residues per subunit has been built and refined to 2.28 Å resolution. It shows mostly helical structure and resembles that of avian farnesyl pyrophosphate synthase.

原文英語
頁(從 - 到)2265-2268
頁數4
期刊Acta Crystallographica - Section D Biological Crystallography
59
發行號12
DOIs
出版狀態已發佈 - 12月 2003
對外發佈

ASJC Scopus subject areas

  • 結構生物學

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