X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site

A. Roujeinikova, C. Baldock, W.J. Simon, J. Gilroy, P.J. Baker, A.R. Stuitje, D.W. Rice, A.R. Slabas, J.B. Rafferty

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and β-mercaptoethylamine moieties of the acylated 4′-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.
    Original languageEnglish
    Pages (from-to)825-835
    Number of pages10
    JournalStructure
    Volume10
    DOIs
    Publication statusPublished - 2002

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    Acyl Carrier Protein
    Binding Sites
    X-Rays
    Cysteamine
    Plastics
    Catalytic Domain
    Fatty Acids
    Enzymes
    Proteins

    Cite this

    Roujeinikova, A., Baldock, C., Simon, W. J., Gilroy, J., Baker, P. J., Stuitje, A. R., ... Rafferty, J. B. (2002). X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site. Structure, 10, 825-835. https://doi.org/10.1016/S0969-2126(02)00775-X
    Roujeinikova, A. ; Baldock, C. ; Simon, W.J. ; Gilroy, J. ; Baker, P.J. ; Stuitje, A.R. ; Rice, D.W. ; Slabas, A.R. ; Rafferty, J.B. / X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site. In: Structure. 2002 ; Vol. 10. pp. 825-835.
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    title = "X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site",
    abstract = "Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and β-mercaptoethylamine moieties of the acylated 4′-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.",
    author = "A. Roujeinikova and C. Baldock and W.J. Simon and J. Gilroy and P.J. Baker and A.R. Stuitje and D.W. Rice and A.R. Slabas and J.B. Rafferty",
    year = "2002",
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    pages = "825--835",
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    Roujeinikova, A, Baldock, C, Simon, WJ, Gilroy, J, Baker, PJ, Stuitje, AR, Rice, DW, Slabas, AR & Rafferty, JB 2002, 'X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site' Structure, vol. 10, pp. 825-835. https://doi.org/10.1016/S0969-2126(02)00775-X

    X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site. / Roujeinikova, A.; Baldock, C.; Simon, W.J.; Gilroy, J.; Baker, P.J.; Stuitje, A.R.; Rice, D.W.; Slabas, A.R.; Rafferty, J.B.

    In: Structure, Vol. 10, 2002, p. 825-835.

    Research output: Contribution to JournalArticleAcademicpeer-review

    TY - JOUR

    T1 - X-Ray Crystallographic Studies on Butyryl-ACP Reveal Flexibility of the Structure around a Putative Acyl Chain Binding Site

    AU - Roujeinikova, A.

    AU - Baldock, C.

    AU - Simon, W.J.

    AU - Gilroy, J.

    AU - Baker, P.J.

    AU - Stuitje, A.R.

    AU - Rice, D.W.

    AU - Slabas, A.R.

    AU - Rafferty, J.B.

    PY - 2002

    Y1 - 2002

    N2 - Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and β-mercaptoethylamine moieties of the acylated 4′-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.

    AB - Acyl carrier protein (ACP) is an essential cofactor in biosynthesis of fatty acids and many other reactions that require acyl transfer steps. We have determined the first crystal structures of an acylated form of ACP from E. coli, that of butyryl-ACP. Our analysis of the molecular surface of ACP reveals a plastic hydrophobic cavity in the vicinity of the phosphopantethylated Ser36 residue that is expanded and occupied by the butyryl and β-mercaptoethylamine moieties of the acylated 4′-phosphopantetheine group in one of our crystal forms. In the other form, the cavity is contracted, and we propose that the protein has adopted the conformation after delivery of substrate into the active site of a partner enzyme.

    U2 - 10.1016/S0969-2126(02)00775-X

    DO - 10.1016/S0969-2126(02)00775-X

    M3 - Article

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