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 Cited by 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: 19782157DOI: 10.1016/j.bbapap.2009.09.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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