Computer simulation of spermine-porin channel interactions.
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.
Vidal
Stéphanie
S
GERCTOP, UMR CNRS 6009, Université de la Méditerranée, 13385 Marseille, France.
Brouant
Pierre
P
Chevalier
Jacqueline
J
Malléa
Monique
M
Barbe
Jacques
J
Pagès
Jean-Marie
JM
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
D029968:Escherichia coli Proteins; C109237:OmpF protein; D018272:Porins; D011994:Recombinant Proteins; D013096:Spermine