title: An analysis of the conformational paths of citrate synthase.
abstract: Previous simulation studies have provided reaction pathways leading from the closed to the open form of citrate synthase. We now undertake a detailed analysis of these pathways using a variety of different tools including backbone dihedral angles, P-Curves helicoidal parameters, inter-helix geometrical parameters, and accessibility calculations. The results point to a relatively small number of residues, mostly in loop regions, which are responsible for the majority of the conformational changes observed. An important role is attributed to transient changes in the backbone which facilitate movement along the reaction coordinate. Comparisons between the two pathways show that they share many common features despite the different algorithms used to generate them.
authors.affiliation: Laboratoire de Physique Quantique CNRS URA505, Université Paul Sabatier, Toulouse, France.
authors.forename: M A
authors.initials: MA
authors.lastname: Ech-Cherif el-Kettani
authors.forename: K
authors.initials: K
authors.lastname: Zakrzewska
authors.forename: J
authors.initials: J
authors.lastname: Durup
authors.forename: R
authors.initials: R
authors.lastname: Lavery
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D002950:Citrate (si)-Synthase / Q000737:chemistry* / Q000378:metabolism; D003198:Computer Simulation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013552:Swine; D014961:X-Ray Diffraction
chemical_list: D002950:Citrate (si)-Synthase