Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family
- Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Bernal (Argentina)
- Instituto de Química y Fisicoquímica Biológicas (IQUIFYB), Facultad de Farmacia y Bioquímica (UBA-CONICET), Buenos Aires (Argentina)
- Unité de Biochimie Structurale, Institut Pasteur, Paris (France)
- Unidad de Biofisica (CSIC-UPV/EHU), PO Box 644, E-48080 Bilbao (Spain)
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. 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.
- OSTI ID:
- 22356378
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 10 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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