1HB6

Structure of bovine Acyl-CoA binding protein in orthorhombic crystal form

Summary for 1HB6

• Entry DOI: 10.2210/pdb1hb6/pdb
• Related: 1ACA 1HB8 2ABD
• Descriptor: ACYL-COA BINDING PROTEIN, CADMIUM ION (3 entities in total)
• Functional Keywords: acyl-coenzyme a binding protein, acyl-coa, binding protein
• Biological source: BOS TAURUS (BOVINE)
• Total number of polymer chains: 1
• Total formula weight: 10043.70

Authors

Zou, J.Y.,Kleywegt, G.J.,Bergfors, T.,Knudsen, J.,Jones, T.A. (deposition date: 2001-04-12, release date: 2002-03-11, Last modification date: 2023-12-13)

Primary citation

Van Aalten, D.M.F.,Milne, K.G.,Zou, J.Y.,Kleywegt, G.J.,Bergfors, T.,Ferguson, M.A.J.,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-, 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)