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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

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

Team: Structural Microbiology
Member: Pedro Alzari
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 30 Sep 2006

Costabel MD, Ermácora MR, Santomé JA, Alzari PM, Guérin DM

Link to Pubmed [PMID] – 17012783

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2006 Oct;62(Pt 10):958-61

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.