Open AccessStructure of armadillo ACBP: a new member of the acyl‐CoA‐binding protein family
Author(s) -
Costabel Marcelo D.,
Alzari Pedro M.,
Ermácora Mario R.,
Santomé José A.,
Guérin Diego M. A.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106038164
Subject(s) - armadillo , harderian gland , biochemistry , chemistry , lipid metabolism , yeast , structural motif , biology , stereochemistry , microbiology and biotechnology , endocrinology
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 α‐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.