3FP5

Crystal structure of ACBP from Moniliophthora perniciosa

Summary for 3FP5

• Entry DOI: 10.2210/pdb3fp5/pdb
• Descriptor: Acyl-CoA Binding Protein, ZINC ION, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: acbp, moniliophthora perniciosa, cacao disease, fatty acid metabolism, lipid binding protein
• Biological source: Moniliophthora perniciosa
• Total number of polymer chains: 1
• Total formula weight: 12375.47

Authors

Monzani, P.S.,Pereira, H.M.,Melo, F.A.,Meirelles, F.V.,Oliva, G.,Cascardo, J.C.M. (deposition date: 2009-01-04, release date: 2009-11-17, Last modification date: 2023-09-06)

Primary citation

Monzani, P.S.,Pereira, H.M.,Melo, F.A.,Meirelles, F.V.,Oliva, G.,Cascardo, J.C.
A new topology of ACBP from Moniliophthora perniciosa.
Biochim.Biophys.Acta, 1804:115-123, 2010

PubMed Abstract: Acyl-CoA binding protein (ACBP) is a housekeeping protein and is an essential protein in human cell lines and in Trypanosoma brucei. The ACBP of Moniliophthora perniciosa is composed of 104 amino acids and is possibly a non-classic isoform exclusively from Basidiomycetes. The M. perniciosa acbp gene was cloned, and the protein was expressed and purified. Acyl-CoA ester binding was analyzed by isoelectric focusing, native gel electrophoresis and isothermal titration calorimetry. Our results suggest an increasing affinity of ACBP for longer acyl-CoA esters, such as myristoyl-CoA to arachidoyl-CoA, and best fit modeling indicates two binding sites. ACBP undergoes a shift from a monomeric to a dimeric state, as shown by dynamic light scattering, fluorescence anisotropy and native gel electrophoresis in the absence and presence of the ligand. The protein's structure was determined at 1.6 A resolution and revealed a new topology for ACBP, containing five alpha-helices instead of four. alpha-helices 1, 2, 3 and 4 adopted a bundled arrangement that is unique from the previously determined four-helix folds of ACBP, while alpha-helices 1, 2, 4 and 5 formed a classical four-helix bundle. A MES molecule was found in the CoA binding site, suggesting that the CoA site could be a target for small compound screening.

PubMed: 19782157
DOI: 10.1016/j.bbapap.2009.09.020

Experimental method

X-RAY DIFFRACTION (1.61 Å)