Biochimie 1998 May-Jun;80(5-6):543-51

Detergent binding in trigonal crystals of OmpF porin from Escherichia coli.

Penel S, Pebay-Peyroula E, Rosenbusch J, Rummel G, Schirmer T, Timmins PA
 

• Institut Laue-Langevin, BP 156, 38042 Grenoble Cedex 9, France;
• Institut de Biologie Structurale/CEA-CNRS and Universite Jospeh Fourier, 41 ave. des Martyrs, 38042 Grenoble Cedex 9, France;
• Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland

Go to the related web page

    The structure of the detergent, ocytyl hydroxyethylsufoxide (C8(HE)SO), bound to the OmpF porin from E coli (in the trigonal crystal form) has been determined by neutron crystallography. Due to a dynamic exchange of detergent molecules with their environment they are not ordered on an atomic scale. The structure reported here is therefore at a resolution of approximately 16 A. The X-ray crystallographically determined structure of the protein provides a starting point for the neutron analysis in which the detergent is visualized primarily thanks to its high contrast against D2O.

    The structure shows the detergent to be located mainly in two areas. It forms toroidal annuli around each OmpF trimer, these annuli fusing to form a detergent belt surrounding a solvent filled column traversing the crystal. Those areas of the protein to which the detergent binds are formed almost exclusively of hydrophobic residues and form a band about 30 A high around the trimer. Its upper and lower bounds are defined by two bands of aromatic residues, tyrosines pointing away from the detergent belt and interacting with the polar headgroups while phenylalanines point inwards. This strongly suggests that the same areas define, in vivo, the location at which protein interacts with lipid. The hydrophobic moiety of detergent is also found mediating the hydrophobic protein-protein interactions at the interface between two trimers on the crystallographic two-fold axis.
Back to Home Page