2FDQ
crystal structure of ACBP from Armadillo Harderian Gland
Summary for 2FDQ
Entry DOI | 10.2210/pdb2fdq/pdb |
Descriptor | Acyl-CoA-binding protein (2 entities in total) |
Functional Keywords | acbp, diazepam binding inhibitor, transport protein |
Biological source | Chaetophractus villosus (large hairy armadillo) |
Total number of polymer chains | 3 |
Total formula weight | 29724.70 |
Authors | Costabel, M.D.,Guerin, D.M.A. (deposition date: 2005-12-14, release date: 2006-10-24, Last modification date: 2023-08-30) |
Primary citation | Costabel, M.D.,Ermacora, M.R.,Santome, J.A.,Alzari, P.M.,Guerin, D.M. Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family. Acta Crystallogr.,Sect.F, 62:958-961, 2006 Cited by PubMed Abstract: The X-ray structure of the tetragonal form of apo acyl-CoA-binding protein (ACBP) from the Harderian gland of the South American armadillo Chaetophractus villosus has been solved. ACBP is a carrier for activated long-chain fatty acids and has been associated with many aspects of lipid metabolism. Its secondary structure is highly similar to that of the corresponding form of bovine ACBP and exhibits the unique flattened alpha-helical bundle (up-down-down-up) motif reported for animal, yeast and insect ACBPs. Conformational differences are located in loops and turns, although these structural differences do not suffice to account for features that could be related to the unusual biochemistry and lipid metabolism of the Harderian gland. PubMed: 17012783DOI: 10.1107/S1744309106038164 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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