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Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family

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.
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Submitted on : Thursday, February 11, 2021 - 6:04:28 PM
Last modification on : Saturday, March 20, 2021 - 3:18:58 AM

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Marcelo Costabel, Mario Ermácora, José Santomé, Pedro Alzari, Diego Guérin. Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2006, 62 (10), pp.958-961. ⟨10.1107/S1744309106038164⟩. ⟨pasteur-03139238⟩

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