The secondary structure in solution of acyl-coenzyme A binding protein from bovine liver using 1H nuclear magnetic resonance spectroscopy.
Acyl-coenzyme A binding protein from bovine liver and the protein expressed in Escherichia coli by the recombinant gene of this protein have been studied by two-dimensional 1H nuclear magnetic resonance spectroscopy. This protein has, in addition to the ability to bind acyl-coenzyme A, been reported to have several important physiological and biochemical functions. It is known as the diazepam binding inhibitor, as a putative neurotransmitter, as a regulator of insulin release from pancreatic cells, and as a mediator in corticotropin-dependent adrenal steroidogenesis. The only difference between the protein produced by recombinant techniques and the native acyl-coenzyme A binding protein is the N-terminal acetyl group present only in the native protein. The two proteins have 86 amino acid residues and a molecular mass of approximately 10,000 Da. Complete assignment of the 1H nuclear magnetic resonances has been obtained for a major proportion of the amino acid residues (55 residues), and partial assignment has been achieved for the others (31 residues). Sequential nuclear Overhauser effects have demonstrated that the protein has a secondary structure consisting of four alpha-helices of residues 1-15, 22-35, 52-60, and 68-85. Furthermore, a large number of long-range nuclear Overhauser effects have been identified, indicating that the assignment given here will provide a basis for a structure determination of this protein in solution by nuclear magnetic resonance spectroscopy.
Andersen
K V
KV
Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, Copenhagen Valby, Denmark.
Ludvigsen
S
S
Mandrup
S
S
Knudsen
J
J
Poulsen
F M
FM
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry*; D002417:Cattle; D050556:Fatty Acid-Binding Proteins; D008099:Liver / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D009363:Neoplasm Proteins; D011487:Protein Conformation; D012996:Solutions
D000596:Amino Acids; D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D012996:Solutions