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. 2006 Oct 1;62(Pt 10):958-61.
doi: 10.1107/S1744309106038164. Epub 2006 Sep 30.

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

Marcelo D Costabel  1 , Mario R Ermácora, José A Santomé, Pedro M Alzari, Diego M A Guérin
Affiliations

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

Marcelo D Costabel et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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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Figures

Figure 1
Figure 1
Crystals of armadillo ACBP. The crystals are approximately 0.3 × 0.3 × 0.3 mm in size.
Figure 2
Figure 2
Stereo image of the crystal structure of armadillo ACBP. Amino acids shown as stick models correspond to sequence differences between armadillo and bovine ACBP. The largest conformational difference between these two proteins is in the loop containing Asn14 (see text).
Figure 3
Figure 3
Stereo image of the loop containing the surface-exposed residues Met46 and Leu47.
See this image and copyright information in PMC

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