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  • 1
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of the Clostridium thermocellum cellulosome xylanase Z feruloyl esterase domain (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1027-1029 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Feruloyl esterases cleave ferulic acid from arabinoxylan and pectin. Feruloyl groups are believed to crosslink the polysaccharide chain within the polymer and to link hemicellulose to lignin, which may play a role in controlling the growth of plants. The Clostridium thermocellum cellulosome xylanase Z feruloyl esterase was expressed in Escherichia coli, purified and crystallized. The crystals diffract to 2.4 Å resolution and belong to the orthorhombic space group P212121, with unit-cell parameters a = 43.14, b = 63.77, c = 79.57 Å. Assuming one molecule per asymmetric unit, the Matthews coefficient is calculated to be 1.87 Å3 Da−1, which corresponds to a solvent content of 34%.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900006521
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray diffraction analysis of the mitochondrial transcription factor sc-mtTFB from Saccharomyces cerevisiae (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 902-903 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Eukaryotic mitochondria contain a distinct mini-chromosome. In yeast, transcription of the mitochondrial genome is mediated by a nuclear-encoded RNA polymerase consisting of a single polypeptide core enzyme and a specificity factor termed sc-mtTFB which bears some similarity to bacterial σ-factors. sc-mtTFB from Saccharomyces cerevisiae has been cloned, expressed, purified and crystallized. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 89.7, b = 44.6, c = 98.9 Å, β = 110°. Based on one molecule per asymmetric unit, the solvent content is estimated to be 48%. Small crystals of dimensions 0.01 × 0.05 × 0.13 mm diffract to at least 2.7 Å resolution on a rotating-anode X-ray source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444900005060
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  • 3
    Electronic Resource
    Electronic Resource
    Selection and characterization of Yersinia pestis YopN mutants that constitutively block Yop secretion (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 57 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Secretion of Yop effector proteins by the Yersinia pestis plasmid pCD1-encoded type III secretion system (T3SS) is regulated in response to specific environmental signals. Yop secretion is activated by contact with a eukaryotic cell or by growth at 37°C in the absence of calcium. The secreted YopN protein, the SycN/YscB chaperone and TyeA form a cytosolic YopN/SycN/YscB/TyeA complex that is required to prevent Yop secretion in the presence of calcium and prior to contact with a eukaryotic cell. The mechanism by which these proteins prevent secretion and the subcellular location where the block in secretion occurs are not known. To further investigate both the mechanism and location of the YopN-dependent block, we isolated and characterized several YopN mutants that constitutively block Yop secretion. All the identified amino-acid substitutions that resulted in a constitutive block in Yop secretion mapped to a central domain of YopN that is not directly involved in the interaction with the SycN/YscB chaperone or TyeA. The YopN mutants required an intact TyeA-binding domain and TyeA to block secretion, but did not require an N-terminal secretion signal, an intact chaperone-binding domain or the SycN/YscB chaperone. These results suggest that a C-terminal domain of YopN complexed with TyeA blocks Yop secretion from a cytosolic, not an extracellular, location. A hypothetical model for how the YopN/SycN/YscB/TyeA complex regulates Yop secretion is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04738.x
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  • 4
    Electronic Resource
    Electronic Resource
    Crystal structure and absolute configuration of the indole alkaloid arborescidine C (1998)
    Springer
    Journal of chemical crystallography 28 (1998), S. 23-26 
    Details
    ISSN: 1572-8854
    Keywords: Arborescidine ; indole alkaloid ; marine compound ; absolute configuration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Notes: Abstract The structure and absolute configuration (3R, 17R) of the indole alkaloid arborescidine C were determined by x-ray diffraction. The six-membered ring assumes a half-chair conformation and the seven-membered ring has a twist-like conformation. The crystal packing is characterized by intermolecular hydrogen-bonding between the hydroxyl group and nitrogen atom N4 which leads to the formation of infinite chains of molecules along the a-axis of the crystal. The absolute configurations of two related indole alkaloids, arborescidine B and arborescidine D are inferred from the experimentally determined configuration of arborescidin C molecule. A comparison of the present structure with that of a related indole alkaloid akagerine showed significant conformational and configurational differences. Crystal data: C16H19N2OBr, orthorhombic, P21212, a = 10.3376(8), b = 15.461(4), c = 9.2094(9)Å, V = 1471.9(6)Å3, Z = 4, D calc = 1.510 g cm−3, λ = 1.54178Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1021770401042
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    Paper (German National Licenses)
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