Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein

D. M. F. van Aalten, K. G. Milne, J. Y. Zou, G. J. Kleywegt, T. Bergfors, Michael A. J. Ferguson, J. Knudsen, T. A. Jones

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    Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 Angstrom resolution crystal structures of a P, falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures published previously; however, the bovine and parasite ACBP structures are less similar. The parasite ACBP is shown to have a different Ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. Several non-conservative differences in residues that interact with the ligand were identified between the mammalian and parasite ACBPs. These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site. (C) 2001 Academic Press.

    Original languageEnglish
    Pages (from-to)181-192
    Number of pages12
    JournalJournal of Molecular Biology
    Issue number1
    Publication statusPublished - 25 May 2001

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