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

• Published in: European journal of biochemistry Vol. 175; no. 1; pp. 9 - 15
• Main Authors: HOLAK, Tadeusz A., NILGES, Michael, PRESTEGARD, James H., GRONENBORN, Angela M., CLORE, G. Marius
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 15.07.1988; Blackwell
• Subjects: Acyl Carrier Protein; Algorithms; Biological and medical sciences; Computer Simulation; Escherichia coli; Fundamental and applied biological sciences. Psychology; Macromolecular Substances; Magnetic Resonance Spectroscopy; Molecular biophysics; N.M.R; Protein Conformation; Solutions; Structure in molecular biology; Tridimensional structure; Acyl; NMR spectrometry; Carrier protein; Solution; Conformation
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1988.tb14159.x

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 ≊ 150° to helix 1. The smaller helix 3 (residues 56–63) is at an angle of ≊ 100° to helix 4.