Structure of armadillo ACBP: a new member of the acyl-CoA-binding protein family.
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.
Costabel
Marcelo D
MD
Grupo de Biofísica, Departamento de Física, Universidad Nacional del Sur, Bahía Blanca, Argentina. costabel@criba.edu.ar
Ermácora
Mario R
MR
Santomé
José A
JA
Alzari
Pedro M
PM
Guérin
Diego M A
DM
D000818:Animals; D001135:Armadillos / Q000378:metabolism*; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D026261:Diazepam Binding Inhibitor / Q000737:chemistry*; D006243:Harderian Gland / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation
D026261:Diazepam Binding Inhibitor