X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site

Anna Roujeinikova, Clair Baldock, William J. Simon, John Gilroy, Patrick J. Baker, Antoine R. Stuitje, David W. Rice, Antoni R. Slabas, John B. Rafferty

    Research output: Contribution to journalArticlepeer-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
    Issue number6
    DOIs
    Publication statusPublished - 2002

    Keywords

    • Acyl carrier protein
    • Acyl chain binding
    • Binding pocket
    • Conformational changes
    • Crystal structure
    • Fatty acid biosynthesis

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