title: Three-dimensional structure of fatty-acid-binding protein from bovine heart.
abstract: The complex of fatty-acid-binding protein (FABP) from bovine heart (cFABP, pI4.9) with endogenous lipid was crystallized in the presence of ammonium sulfate as precipitant. The needle-shaped crystals belong to the monoclinic space group C2, with unit-cell constants a = 5.262(6) nm, b = 7.631(8) nm, c = 3.945(5) nm and beta = 94.47(9) degrees. A native data set to 0.35 nm resolution was collected using synchrotron radiation and film methods. An initial model for the three-dimensional structure of the protein was constructed based on the crystal structure of the related bovine P2 myelin protein [Jones, T.A., Bergfors, T., Sedzik, J. & Unge, T. (1988) EMBO J. 7, 1597-1604] to which the amino acid sequence of bovine cFABP was adapted. Energy minimizations were carried out under different conditions using both an all-atom and a united-atom force field. The optimized models were used to determine the crystal structure of cFABP by molecular-replacement techniques. The structure was refined by simulated annealing to R = 0.267. As the bound lipid is heterogeneous, it could not be located in the electron-density map and/or the attained resolution was not sufficient. Bovine cFABP is composed of ten antiparallel beta strands forming a beta barrel, and by two alpha helices. The structural features are similar to those of other members of the superfamily of hydrophobic molecule transporters.
authors.affiliation: Institut für Kristallographie, Freie Universität Berlin, Federal Republic of Germany.
authors.forename: A
authors.initials: A
authors.lastname: Müller-Fahrnow
authors.forename: U
authors.initials: U
authors.lastname: Egner
authors.forename: T A
authors.initials: TA
authors.lastname: Jones
authors.forename: H
authors.initials: H
authors.lastname: Rüdel
authors.forename: F
authors.initials: F
authors.lastname: Spener
authors.forename: W
authors.initials: W
authors.lastname: Saenger
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002417:Cattle; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009206:Myocardium / Q000378:metabolism*; D009363:Neoplasm Proteins; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
chemical_list: D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D005227:Fatty Acids; D009363:Neoplasm Proteins