title: Three-dimensional structure of acyl carrier protein in solution determined by nuclear magnetic resonance and the combined use of dynamical simulated annealing and distance geometry.
abstract: The solution conformation of acyl carrier protein from Escherichia coli (77 residues) has been determined on the basis of 423 interproton-distance restraints and 32 hydrogen-bonding restraints derived from NMR measurements. A total of nine structures were computed using a hybrid approach combining metric matrix distance geometry and dynamic simulated annealing. The polypeptide fold is well defined with an average backbone atomic root-mean-square difference of 0.20 +/- 0.03 nm between the final nine converged structures and the mean structure obtained by averaging their coordinates. The principal structural motif is composed of three helices: 1 (residues 3-12), 2 (residues 37-47) and 4 (residues 65-75) which line a hydrophobic cavity. Helices 2 and 4 are approximately parallel to each other and anti-parallel at an angle of approximately equal to 150 degrees to helix 1. The smaller helix 3 (residues 56-63) is at an angle of approximately equal to 100 degrees to helix 4.
authors.affiliation: Max-Planck-Institut für Biochemie, Martinsried bei München.
authors.forename: T A
authors.initials: TA
authors.lastname: Holak
authors.forename: M
authors.initials: M
authors.lastname: Nilges
authors.forename: J H
authors.initials: JH
authors.lastname: Prestegard
authors.forename: A M
authors.initials: AM
authors.lastname: Gronenborn
authors.forename: G M
authors.initials: GM
authors.lastname: Clore
mesh_terms: D000213:Acyl Carrier Protein; D000465:Algorithms; D003198:Computer Simulation; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D012996:Solutions
chemical_list: D000213:Acyl Carrier Protein; D046911:Macromolecular Substances; D012996:Solutions