1hbk
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ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM
OverviewOverview
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 A 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.
About this StructureAbout this Structure
1HBK is a Protein complex structure of sequences from Plasmodium falciparum with NI, COA and MYR as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
ReferenceReference
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein., van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA, J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287
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