Cobalt-, zinc- and iron-bound forms of adenylate kinase (AK) from the sulfate-reducing bacterium Desulfovibrio gigas: purification, crystallization and preliminary X-ray diffraction analysis

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Abstract

Adenylate kinase (AK; ATP:AMP phosphotransferase; EC 2.7.4.3) is involved in the reversible transfer of the terminal phosphate group from ATP to AMP. AKs contribute to the maintenance of a constant level of cellular adenine nucleotides, which is necessary for the energetic metabolism of the cell. Three metal ions, cobalt, zinc and iron(II), have been reported to be present in AKs from some Gram-negative bacteria. Native zinc-containing AK from Desulfovibrio gigas was purified to homogeneity and crystallized. The crystals diffracted to beyond 1.8 angstrom resolution. Furthermore, cobalt-and iron-containing crystal forms of recombinant AK were also obtained and diffracted to 2.0 and 3.0 angstrom resolution, respectively. Zn2+-AK and Fe2+-AK crystallized in space group I222 with similar unit-cell parameters, whereas Co2+-AK crystallized in space group C2; a monomer was present in the asymmetric unit for both the Zn2+-AK and Fe2+-AK forms and a dimer was present for the Co2+-AK form. The structures of the three metal-bound forms of AK will provide new insights into the role and selectivity of the metal in these enzymes.
Original languageUnknown
Pages (from-to)926-929
JournalActa Crystallographica Section F-Structural Biology And Crystallization Com
Volume65
Issue numberNA
DOIs
Publication statusPublished - 1 Jan 2009

Keywords

    Cite this

    @article{efa44d17ccfa4beeb9698e1c6f76cfe1,
    title = "Cobalt-, zinc- and iron-bound forms of adenylate kinase (AK) from the sulfate-reducing bacterium Desulfovibrio gigas: purification, crystallization and preliminary X-ray diffraction analysis",
    abstract = "Adenylate kinase (AK; ATP:AMP phosphotransferase; EC 2.7.4.3) is involved in the reversible transfer of the terminal phosphate group from ATP to AMP. AKs contribute to the maintenance of a constant level of cellular adenine nucleotides, which is necessary for the energetic metabolism of the cell. Three metal ions, cobalt, zinc and iron(II), have been reported to be present in AKs from some Gram-negative bacteria. Native zinc-containing AK from Desulfovibrio gigas was purified to homogeneity and crystallized. The crystals diffracted to beyond 1.8 angstrom resolution. Furthermore, cobalt-and iron-containing crystal forms of recombinant AK were also obtained and diffracted to 2.0 and 3.0 angstrom resolution, respectively. Zn2+-AK and Fe2+-AK crystallized in space group I222 with similar unit-cell parameters, whereas Co2+-AK crystallized in space group C2; a monomer was present in the asymmetric unit for both the Zn2+-AK and Fe2+-AK forms and a dimer was present for the Co2+-AK form. The structures of the three metal-bound forms of AK will provide new insights into the role and selectivity of the metal in these enzymes.",
    keywords = "motions, binding",
    author = "Moura, {Jos{\'e} Jo{\~a}o Galhardas de} and Bursakov, {Sergey Alekseevitch} and Moura, {Isabel Maria Andrade Martins Galhardas de} and Rom{\~a}o, {Maria Jo{\~a}o}",
    year = "2009",
    month = "1",
    day = "1",
    doi = "10.1107/S1744309109029157",
    language = "Unknown",
    volume = "65",
    pages = "926--929",
    journal = "Acta Crystallographica Section F-Structural Biology And Crystallization Com",
    issn = "1744-3091",
    publisher = "Blackwell Publishing Ltd",
    number = "NA",

    }

    TY - JOUR

    T1 - Cobalt-, zinc- and iron-bound forms of adenylate kinase (AK) from the sulfate-reducing bacterium Desulfovibrio gigas: purification, crystallization and preliminary X-ray diffraction analysis

    AU - Moura, José João Galhardas de

    AU - Bursakov, Sergey Alekseevitch

    AU - Moura, Isabel Maria Andrade Martins Galhardas de

    AU - Romão, Maria João

    PY - 2009/1/1

    Y1 - 2009/1/1

    N2 - Adenylate kinase (AK; ATP:AMP phosphotransferase; EC 2.7.4.3) is involved in the reversible transfer of the terminal phosphate group from ATP to AMP. AKs contribute to the maintenance of a constant level of cellular adenine nucleotides, which is necessary for the energetic metabolism of the cell. Three metal ions, cobalt, zinc and iron(II), have been reported to be present in AKs from some Gram-negative bacteria. Native zinc-containing AK from Desulfovibrio gigas was purified to homogeneity and crystallized. The crystals diffracted to beyond 1.8 angstrom resolution. Furthermore, cobalt-and iron-containing crystal forms of recombinant AK were also obtained and diffracted to 2.0 and 3.0 angstrom resolution, respectively. Zn2+-AK and Fe2+-AK crystallized in space group I222 with similar unit-cell parameters, whereas Co2+-AK crystallized in space group C2; a monomer was present in the asymmetric unit for both the Zn2+-AK and Fe2+-AK forms and a dimer was present for the Co2+-AK form. The structures of the three metal-bound forms of AK will provide new insights into the role and selectivity of the metal in these enzymes.

    AB - Adenylate kinase (AK; ATP:AMP phosphotransferase; EC 2.7.4.3) is involved in the reversible transfer of the terminal phosphate group from ATP to AMP. AKs contribute to the maintenance of a constant level of cellular adenine nucleotides, which is necessary for the energetic metabolism of the cell. Three metal ions, cobalt, zinc and iron(II), have been reported to be present in AKs from some Gram-negative bacteria. Native zinc-containing AK from Desulfovibrio gigas was purified to homogeneity and crystallized. The crystals diffracted to beyond 1.8 angstrom resolution. Furthermore, cobalt-and iron-containing crystal forms of recombinant AK were also obtained and diffracted to 2.0 and 3.0 angstrom resolution, respectively. Zn2+-AK and Fe2+-AK crystallized in space group I222 with similar unit-cell parameters, whereas Co2+-AK crystallized in space group C2; a monomer was present in the asymmetric unit for both the Zn2+-AK and Fe2+-AK forms and a dimer was present for the Co2+-AK form. The structures of the three metal-bound forms of AK will provide new insights into the role and selectivity of the metal in these enzymes.

    KW - motions

    KW - binding

    U2 - 10.1107/S1744309109029157

    DO - 10.1107/S1744309109029157

    M3 - Article

    VL - 65

    SP - 926

    EP - 929

    JO - Acta Crystallographica Section F-Structural Biology And Crystallization Com

    JF - Acta Crystallographica Section F-Structural Biology And Crystallization Com

    SN - 1744-3091

    IS - NA

    ER -