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

Octaprenyl pyrophosphate synthase (OPPs) catalyzes the condensation of five isopentenyl pyrophosphates with farnesyl pyrophosphate to generate C40 octaprenyl pyrophosphate. The enzymes from the hyperthermophilic bacterium Thermotoga maritima and from the mesophilic Escherichia coli were expressed in...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-12, Vol.59 (12), p.2265-2268
Hauptverfasser: Guo, Rey-Ting, Ko, Tzu-Ping, Chou, Chia-Cheng, Shr, Hui-Lin, Chu, Hsing-Mao, Tsai, Yao-Hsien, Liang, Po-Huang, Wang, Andrew H.-J.
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Sprache:eng
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Zusammenfassung:Octaprenyl pyrophosphate synthase (OPPs) catalyzes the condensation of five isopentenyl pyrophosphates with farnesyl pyrophosphate to generate C40 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 P4212, 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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444903018985