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  • 1
    Electronic Resource
    Electronic Resource
    The structure and domain organization of Escherichia coli isocitrate lyase (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1209-1218 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Enzymes of the glyoxylate-bypass pathway are potential targets for the control of many human diseases caused by such pathogens as Mycobacteria and Leishmania. Isocitrate lyase catalyses the first committed step in this pathway and the structure of this tetrameric enzyme from Escherichia coli has been determined at 2.1 Å resolution. E. coli isocitrate lyase, like the enzyme from other prokaryotes, is located in the cytoplasm, whereas in plants, protozoa, algae and fungi this enzyme is found localized in glyoxysomes. Comparison of the structure of the prokaryotic isocitrate lyase with that from the eukaryote Aspergillus nidulans reveals a different domain structure following the deletion of approximately 100 residues from the larger eukaryotic enzyme. Despite this, the active sites of the prokaryotic and eukaryotic enzymes are very closely related, including the apparent disorder of two equivalent segments of the protein that are known to be involved in a conformational change as part of the enzyme's catalytic cycle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901008642
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  • 2
    Electronic Resource
    Electronic Resource
    Crystallization of the NAD(P)-dependent glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 240-242 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The NAD(P)-dependent glutamate dehydrogenase from Pyrococcus furiosus has been crystallized by the hanging-drop method of vapour diffusion using lithium sulfate as the precipitant. The crystals belong to the tetragonal system and are in space group P42212 with unit-cell dimensions of a = b = 167.2, c = 172.9 Å. Consideration of the values of Vm and possible packing of the molecules within the cell suggest that the asymmetric unit contains a trimer. P. furiosus belongs to the family of Archaea and is one of the most thermostable organisms known, having an optimal growth temperature of 376 K. The glutamate dehydrogenase isolated from this organism has a half-life of 12 h at 373 K and, therefore, the determination of the structure of this enzyme will be important in advancing our understanding of how proteins are adapted to enable them to survive at such extreme temperatures.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994012862
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  • 3
    Electronic Resource
    Electronic Resource
    Crystallization of the glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1185-1187 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The NADP+-dependent glutamate dehydrogenase from Thermococcus litoralis has been crystallized by the hanging-drop method of vapour diffusion using an ammonium sulfate and PEG mixture as the precipitant. The crystals belong to the monoclinic system and are in space group C2 with unit-cell dimensions a = 142.7, b = 202.0, c = 125.8 Å with β = 113.1° with a hexamer in the asymmetric unit. T. Litoralis, a hyperthermophilic organism, belongs to the family of Archaea and has a maximum growth temperature of about 370 K. The glutamate dehydrogenase isolated from this organism has a half-life of 2 h at 373 K and a comparison of this structure with that of other GluDH's from hyperthermophilic organisms and from mesophiles will contribute to an understanding of the molecular mechanisms which underlie thermostability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996007421
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallization of Escherichia coli enoyl reductase and its complex with diazaborine (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1181-1184 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Recent work has shown that the NADH-dependent enoyl acyl carrier protein reductase from Escherichia coli is the target for diazaborine, an antibacterial agent. This enzyme has been crystallized by the hanging-drop method of vapour diffusion complexed with NAD+ and in the presence and absence of a thieno diazaborine. The crystals grown in the absence of diazaborine (form A) are in the space group P21 with unit-cell dimensions a = 74.0, b = 81.2, c = 79.0 Å and β = 92.9°, and with a tetramer in the asymmetric unit, whilst those grown in the presence of diazaborine (form B) are in the space group P6122 (or P6522) with unit-cell dimensions a = b = 80.9 and c = 328.3 Å, and with a dimer in the asymmetric unit. The structure determination of this enzyme in the presence of diazaborine will provide information on the nature of the drug binding site and contribute to a programme of rational drug design.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996005458
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray analysis of the glycerol-3-phosphate 1-acyltransferase from squash (Cucurbita moschata) (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 451-453 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Glycerol-3-phosphate 1-acyltransferase (E.C. 2.3.1.15; G3PAT) catalyses the incorporation of an acyl group from either acyl-acyl carrier proteins (acylACPs) or acylCoAs into the sn-1 position of glycerol 3-phosphate to yield 1-acylglycerol 3-phosphate. Crystals of squash G3PAT have been obtained by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant. These crystals are most likely to belong to space group P212121, with approximate unit-cell parameters a = 61.1, b = 65.1, c = 103.3 Å, α = β = γ = 90° and a monomer in the asymmetric unit. X-ray diffraction data to 1.9 Å resolution have been collected in-house using a MAR 345 imaging-plate system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901000257
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  • 6
    Electronic Resource
    Electronic Resource
    Crystallization of E. coli RuvA gives insights into the symmetry of a Holliday junction/protein complex (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 122-124 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The E. coli protein RuvA (resistance to ultraviolet light) has been overexpressed in E. coli, purified and crystallized using the hanging-drop vapour-diffusion method with sodium chloride as the precipitant. The crystals, which diffract to beyond 1.9 Å, belong to the tetragonal system, space group P4 with unit-cell dimensions of a = 83.7, c = 33.1 Å with a monomer in the asymmetric unit. RuvA is known to be a tetramer and thus the crystal symmetry implies that its quaternary structure will be based on fourfold rotation symmetry rather than 222 symmetry. This is consistent with electron microscopy data on Holliday junction DNA complexes and implies that the arms of the four DNA duplexes involved in recombination adopt fourfold rotation symmetry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996009869
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  • 7
    Electronic Resource
    Electronic Resource
    Isocitrate lyase from Aspergillus nidulans: crystallization and X-ray analysis of a glyoxylate cycle enzyme (1997)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 53 (1997), S. 488-490 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Isocitrate lyase (ICL) from the filamentous fungus Aspergillus nidulans catalyzes the first committed step of the carbon-conserving glyoxylate bypass. This enzyme has been crystallized by the hanging-drop method of vapour diffusion using polyethylene glycol 2000 as the precipitant. Diffraction patterns show that the crystals diffract to beyond 2.5 Å and are probably in space group P42212 with unit-cell dimensions of a = b = 91.9 and c = 152.7 Å, with one molecule in the asymmetric unit. The elucidation of the structure of this enzyme to high resolution will advance the understanding of how the metabolic branch point between the tricarboxylic acid cycle and the glyoxylate bypass is controlled by the affinity of ICL for its substrate isocitrate and contribute to a programme of rational drug design.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444997002680
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  • 8
    Electronic Resource
    Electronic Resource
    The complete primary structure of ribosomal protein L1 fromThermus thermophilus (1993)
    Springer
    The protein journal 12 (1993), S. 725-734 
    Details
    ISSN: 1573-4943
    Keywords: Amino acid sequence ; ribosomal protein ; L1 fromThermus thermophilus ; domain structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The primary structure of the 23S rRNA binding ribosomal protein L1 from the 50S ribosomal subunit ofThermus thermophilus ribosomes has been elucidated by direct protein sequencing of selected peptides prepared by enzymatic and chemical cleavage of the intact purified protein. The polypeptide chain contains 228 amino acids and has a calculated molecular mass of 24,694 D. A comparison with the primary structures of the corresponding proteins fromEscherichia coli andBacillus stearothermophilus reveals a sequence homology of 49% and 58%, respectively. With respect to both proteins, L1 fromT. thermophilus contains particularly less Ala, Lys, Gln, and Val, whereas its content of Glu, Gly, His, Ile, and Arg is higher. In addition, two fragments obtained by limited proteolysis of the intact, unmodified protein were characterized.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024930
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