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  • 1
    Electronic Resource
    Electronic Resource
    Toxoplasma gondii adenosine kinase: expression, purification, characterization, crystallization and preliminary crystallographic analysis (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 76-78 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The obligate intracellular protozoan parasite Toxoplasma gondii depends on the purine-salvage pathway for its purine supply. Unlike its mammalian hosts, T. gondii salvages purine precursors predominantly via adenosine kinase, the enzyme that phosphorylates adenosine to adenosine monophosphate (AMP). The cDNA encoding T. gondii adenosine kinase was subcloned and expressed in Escherichia coli. The recombinant protein was active in an in vitro enzyme assay over a broad pH range. It required a divalent cation for activity. The enzyme was inactivated by the addition of 1 µM mercuric chloride. The inactivation could be reversed by a reducing agent. The active recombinant protein was crystallized using sodium sulfate as precipitant at pH 8.0. The crystals diffract to 1.8 Å and belong to the monoclinic space group P21, with unit-cell parameters a = 47.5, b = 68.9, c = 57.0 Å, β = 100.3°. The calculated Vm based on one molecule per asymmetric unit is 2.38 Å3 Da−1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444999013840
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  • 2
    Electronic Resource
    Electronic Resource
    Structure of the nucleotide-binding domain of Plasmodium falciparum Rab6 in the GDP-bound form (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 937-944 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Rab proteins are small Ras-like GTPases which play important roles in regulating intracellular vesicle trafficking. The nucleotide-binding domain of Rab6 from the malaria parasite Plasmodium falciparum was crystallized with GDP bound to the active site. The MAD phasing technique was used to determine the crystal structure to 2.3 Å resolution. Comparisons of the structure of GDP-bound PfRab6 with the recently determined structures of Rab3A in complex with either a GTP analog or with GTP and Rabphillin present structural evidence supporting the traditional model for the molecular GTP/GDP switch in Rab proteins. PfRab6 residues homologous to those distinguishing human Rab6 isoforms, which differ in binding to Rabkinesin-6 in human cells, are located next to the recognized complementarity-determining region (CDR) and constitute a conceptual broadening of that domain. Despite significant observable differences in Golgi ultrastructure, the Rab6 core structure and switch mechanism appear highly conserved when compared with murine Rab3a structures. A significant difference between the PfRab6 and higher eukaryotic Rabs may be the lack of CDR features that allow binding interactions with Rabkinesin-type effectors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900007575
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  • 3
    Electronic Resource
    Electronic Resource
    Structure of human α-thrombin complexed with RWJ-51438 at 1.7 Å: unusual perturbation of the 60A–60I insertion loop (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1395-1400 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional structure of the ternary complex consisting of human α-thrombin, hirugen and the active-site inhibitor RWJ-51438 has been determined at 1.7 Å resolution. The crystals of the complex belong to the orthorhombic space group P21212, with unit-cell parameters a = 62.98, b = 117.52, c = 47.99 Å. The refined R and Rfree values are 0.196 and 0.232, respectively. The ketone carbonyl group of the inhibitor is covalently linked to the hydroxyl O atom of Ser195, forming a tetrahedral intermediate hemiketal structure; the benzothiazole ring N atom of RWJ-51438 forms a hydrogen bond with His57. Surprisingly, the carboxylate substituent on the benzothiazole group forms salt bridges with Lys60F NZ and the NZ of the symmetry-related residues Lys236 and Lys240, which introduces steric effects that perturb the 60A–60I insertion loop, especially at residues Trp60D and Phe60H.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900010763
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  • 4
    Electronic Resource
    Electronic Resource
    7-Chloro-1-(2,6-difluorophenyl)-1H,3H-thiazolo[3,4-a]benzimidazole and 1-(2,6-difluorophenyl)-6-methyl-1H,3H-thiazolo[3,4-a]benzimidazole (2001)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 572-574 
    Details
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The title molecules, C15H9ClF2N2S and C16H12F2N2S, respectively, display the well known butterfly-like conformation with a flat thiazolobenzimidazole system. In both compounds, the mean plane through the tricyclic system is almost perpendicular to the 2,6-difluorophenyl ring. This arrangement of the aryl group is determined by two intramolecular hydrogen bonds and by an attractive F...S interaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108270101001421
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