title: Preliminary X-ray diffraction analysis of octaprenyl pyrophosphate synthase crystals from Thermotoga maritima and Escherichia coli.
abstract: 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 A. The E. coli OPPs crystals belong to space group C222(1), with unit-cell parameters a = 247.66, b = 266.10, c = 157.93 A. 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 A resolution. The asymmetric unit contains one dimer. An initial model with 280 residues per subunit has been built and refined to 2.28 A resolution. It shows mostly helical structure and resembles that of avian farnesyl pyrophosphate synthase.
authors.affiliation: Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan.
authors.forename: Rey-Ting
authors.initials: RT
authors.lastname: Guo
authors.forename: Tzu-Ping
authors.initials: TP
authors.lastname: Ko
authors.forename: Chia-Cheng
authors.initials: CC
authors.lastname: Chou
authors.forename: Hui-Lin
authors.initials: HL
authors.lastname: Shr
authors.forename: Hsing-Mao
authors.initials: HM
authors.lastname: Chu
authors.forename: Yao-Hsien
authors.initials: YH
authors.lastname: Tsai
authors.forename: Po-Huang
authors.initials: PH
authors.lastname: Liang
authors.forename: Andrew H J
authors.initials: AH
authors.lastname: Wang
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D019883:Alkyl and Aryl Transferases