title: Computer simulation of spermine-porin channel interactions.
abstract: Porin channels play a prominent role during fluoroquinolone uptake and spermine strongly alters the diffusion rate of norfloxacine. Consequently the interactions between spermine and bacterial porin were studied by computer simulation. The results indicate that various residues (E62, D 113, E 117,...) closely located in the internal eyelet region of the OmpF channel are potential binding sites. Among them, the D 113 residue, seems to play an important role in the association channel-spermine. This interaction introduces several changes in the internal morphology of the channel which are responsible for the inhibition of antibiotic uptake using the porin route.
authors.affiliation: GERCTOP, UMR CNRS 6009, Université de la Méditerranée, 13385 Marseille, France.
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Vidal
authors.forename: Pierre
authors.initials: P
authors.lastname: Brouant
authors.forename: Jacqueline
authors.initials: J
authors.lastname: Chevalier
authors.forename: Monique
authors.initials: M
authors.lastname: Malléa
authors.forename: Jacques
authors.initials: J
authors.lastname: Barbe
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Pagès
mesh_terms: D001665:Binding Sites; D003198:Computer Simulation; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D016296:Mutagenesis; D018272:Porins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013096:Spermine / Q000737:chemistry* / Q000502:physiology
chemical_list: D029968:Escherichia coli Proteins; C109237:OmpF protein; D018272:Porins; D011994:Recombinant Proteins; D013096:Spermine