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  • Chemistry  (2)
  • Iron/zinc center  (1)
  • streptomyces malayensis  (1)
  • 1
    Digitale Medien
    Digitale Medien
    The 1.9 Å crystal structure of the “as isolated” rubrerythrin from Desulfovibrio vulgaris: some surprising results (2000)
    Springer
    JBIC 5 (2000), S. 505-513 
    Details
    ISSN: 1432-1327
    Schlagwort(e): Key words Non-heme iron ; Iron-cysteine center ; Iron/zinc center ; Hydrogen bonding ; Dinuclear center
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Abstract Rubrerythrin is a non-heme iron dimeric protein isolated from the sulfate-reducing bacterium Desulfovibrio vulgaris. Each monomer has one mononuclear iron center similar to rubredoxin and one dinuclear metal center similar to hemerythrin or ribonucleotide reductase. The 1.88 Å X-ray structure of the “as isolated” molecule and a uranyl heavy atom derivative have been solved by molecular replacement techniques. The resulting model of the native “as isolated” molecule, including 164 water molecules, has been refined giving a final R factor of 0.197 (R free=0.255). The structure has the same general protein fold, domain structure, and dimeric interactions as previously found for rubrerythrin [1, 2], but it also has some interesting undetected differences at the metal centers. The refined model of the protein structure has a cis peptide between residues 78 and 79. The Fe-Cys4 center has a previously undetected strong seventh N-H...S hydrogen bond in addition to the six N-H...S bonds usually found in rubredoxin. The dinuclear metal center has a hexacoordinate Fe atom and a tetracoordinate Zn atom. Each metal is coordinated by a GluXXHis polypeptide chain segment. The Zn atom binds at a site distinctly different from that found in the structure of a diiron rubrerythrin. Difference electron density for the uranyl derivative shows an extremely large peak adjacent to and replacing the Zn atom, indicating that this particular site is capable of binding other atoms. This feature/ability may give rise to some of the confusing activities ascribed to this molecule.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s007750050011
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  • 2
    Digitale Medien
    Digitale Medien
    Crystallization and preliminary X-ray diffraction study of a protein with a high potential rubredoxin center and a hemerythrin-type Fe center (1988)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 3 (1988), S. 184-186 
    Details
    ISSN: 0887-3585
    Schlagwort(e): new Fe-protein ; rubredoxin ; hemerythrin ; crystals ; X-ray diffraction ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: A newly discovered iron-containing protein, isolated from the bacterium Desulfovibrio vulgaris (Hildenborough, NCIB 8303), has been crystallized. The molecule appears to be a dimer of mass 44kDa. This protein has iron centers with spectroscopic similarities to those in rubredoxins and in hemerythrins.The X-ray diffraction shows symmetry consistent with space group I222 or I212121. Cell parameters are a = 49.2 Å, b = 81.3 Å, c= 100.1 Å, and α, β, γ = 90°. X-ray diffraction data have been collected to 3.0 Å, and a search for useful heavy atom derivatives is in progress for the analysis of the crystal structure of this Fe-protein.
    Zusätzliches Material: 1 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/prot.340030306
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  • 3
    Digitale Medien
    Digitale Medien
    Preliminary X-ray diffraction studies and biochemical characterization of the antitumor protein mitomalcin indicate close similarity to neocarzinostatin (1988)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 3 (1988), S. 252-255 
    Details
    ISSN: 0887-3585
    Schlagwort(e): streptomyces malayensis ; antitumor antibiotic ; holoprotein antibiotic ; crystallization of mitomalcin ; amino acid composition ; partial amino acid sequence ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Medizin
    Notizen: The antitumor antibiotic protein mitomalcin, from the microorganism Streptomyces malayensis, has been purified to apparent homogenity and crystallized. The crystals belong to space group P212121 and have the following cell parameters : a=27.2 Å, b=34.1 Å, c=101.7 Å, and alpha;=β=γ=90°. These crystal properties are extremely similar to crystals of the antitumor protein neocarzinostatin (11.7 kilodaltons [kDa]) from Streptomyces carzinostaticus in spite of differing pH conditions for crystallizing the two proteins and an apparent difference in molecular weight is similar to that of neocarzinostatin. An amino acid composition analysis of mitomalcin indicates that some differences may exist between the two molecules, but a preliminary amino acid sequence analysis of the first 37 residues found no difference in the N-terminal region of the molecule.
    Zusätzliches Material: 2 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/prot.340030406
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