Structural highlights
Function
[ACBP_CHAVI] Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family.,Costabel MD, Ermacora MR, Santome JA, Alzari PM, Guerin DM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):958-61. Epub 2006 Sep 30. PMID:17012783[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Costabel MD, Ermacora MR, Santome JA, Alzari PM, Guerin DM. Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Oct 1;62(Pt, 10):958-61. Epub 2006 Sep 30. PMID:17012783 doi:10.1107/S1744309106038164
