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  • 1
    Electronic Resource
    Electronic Resource
    Structure of inhibited trypsin from Fusarium oxysporum at 1.55 Å (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 73-85 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The structure of trypsin from the fungus Fusarium oxysporum has been refined at 1.55 Å resolution by restrained least-squares minimization to an R-factor of 14.4%. The data were recorded from a single-crystal on the X31 beamline at EMBL, Hamburg, using a locally developed image-plate scanner. The final model consists of 1557 protein atoms, 400 water molecules, one molecule of isopropanol and one monoisopropyl phosphoryl inhibitor group covalently bound to the catalytic Ser195. Comparison of the structure with bovine trypsin reveals significant differences in the active site and suggests a possible explanation for the difference in substrate specificity between the two enzymes. In F. oxysporum trypsin the specificity pocket is larger than in bovine trypsin. This explains the preference of F. oxysporum trypsin for the bulkier arginine over lysine and the reverse preference in bovine trypsin. The binding cavity on the C-terminal side of the substrate is more restricted in F. oxysporum trypsin than in mammalian and Streptomyces griseus trypsins, which explains the relative inactivity of F. oxysporum trypsin towards peptide–pNA substrate analogues as an unfavourable steric interaction between the side of the binding cavity and the para-nitroanilino group of peptide–pNA. The observed restriction of the binding cavity does not lead to a reduced catalytic activity compared to other trypsins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994009169
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Preliminary X-ray diffraction studies of the external functional unit RtH2-e from the Rapana thomasiana (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1663-1665 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The `external' oxygenated functional unit RtH2-e of the Rapana hemocyanin subunit RHSS2 was isolated and crystallized. X-ray intensity data to 3.3 Å resolution have been collected at 100 K and the structure has been solved using the molecular-replacement method. The space group is assigned to be the tetragonal P43212, with unit-cell parameters a = b = 105.5, c = 375.0 Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901012124
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  • 3
    Electronic Resource
    Electronic Resource
    The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65-Å resolution (1998)
    Springer
    JBIC 3 (1998), S. 268-273 
    Details
    ISSN: 1432-1327
    Keywords: Key words Urease ; Bacillus pasteurii ; X-ray ; Nickel ; β-Mercaptoethanol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The structure of β-mercaptoethanol-inhibited urease from Bacillus pasteurii, a highly ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic diffraction data. The structure clearly shows the unexpected binding mode of β-mercaptoethanol, which bridges the two nickel ions in the active site through the sulfur atom and chelates one Ni through the OH functionality. Another molecule of inhibitor forms a mixed disulfide with a Cys residue, thus sealing the entrance to the active site cavity by steric hindrance. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050231
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  • 4
    Electronic Resource
    Electronic Resource
    The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution (2000)
    Springer
    JBIC 5 (2000), S. 110-118 
    Details
    ISSN: 1432-1327
    Keywords: Key words Urease ; Bacillus pasteurii ; X-ray diffraction ; Nickel ; Acetohydroxamic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 Å resolution, 99.5% completeness, data redundancy = 26, R-factor = 15.1%, PDB code 4UBP). The two Ni ions in the active site are separated by a distance of 3.53 Å. The structure clearly shows the binding mode of the inhibitor anion, symmetrically bridging the two Ni ions in the active site through the hydroxamate oxygen and chelating one Ni ion through the carbonyl oxygen. The flexible flap flanking the active site cavity is in the open conformation. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050014
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