1HBK

Acyl-CoA binding protein from Plasmodium falciparum

Summary for 1HBK

• Entry DOI: 10.2210/pdb1hbk/pdb
• Descriptor: ACYL-COA BINDING PROTEIN, COENZYME A, MYRISTIC ACID, ... (5 entities in total)
• Functional Keywords: fatty acid metabolism
• Biological source: PLASMODIUM FALCIPARUM
• Total number of polymer chains: 1
• Total formula weight: 11803.39

Authors

van Aalten, D.M.F. (deposition date: 2001-04-16, release date: 2001-05-15, Last modification date: 2024-05-08)

Primary citation

van Aalten, D.M.,Milne, K.G.,Zou, J.Y.,Kleywegt, G.J.,Bergfors, T.,Ferguson, M.A.,Knudsen, J.,Jones, T.A.
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein.
J. Mol. Biol., 309:181-192, 2001

PubMed Abstract: 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.

PubMed: 11491287
DOI: 10.1006/jmbi.2001.4749

Experimental method

X-RAY DIFFRACTION (2 Å)