Low Resolution Structure and Dynamics of a Colicin-Receptor Complex Determined by Neutron Scattering

Clifton, Luke; Johnson, Christopher; Solovyova, Alexandra; Callow, Phil; Weiss, Kevin L.; Ridley, Helen; Le Brun, Anton; Kinane, Christy; Webster, John; Holt, Stephen; Lakey, Jeremy

doi:10.1074/jbc.M111.302901

Title: Low Resolution Structure and Dynamics of a Colicin-Receptor Complex Determined by Neutron Scattering

Journal Article · Mon Jan 02 00:00:00 EST 2012 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.M111.302901· OSTI ID:1032832

Clifton, Luke ^[1]; Johnson, Christopher ^[2]; Solovyova, Alexandra ^[2]; Callow, Phil ^[3];

^[4]; Ridley, Helen ^[2]; Le Brun, Anton ^[2]; Kinane, Christy ^[1]; Webster, John ^[1]; Holt, Stephen ^[1]; Lakey, Jeremy ^[1]

Science and Technology Facilities Council (STFC), Oxford (United Kingdom). Rutherford Appleton Lab., ISIS Neutron Source
Univ. of Newcastle, Newcastle-upon-Tyne (United Kingdom). Inst. for Cell and Molecular Biosciences, The Medical School
Inst. Laue Langevin, Grenoble (France)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Structural Molecular Biology (CSMB)

Proteins that translocate across cell membranes need to overcome a significant hydrophobic barrier. This is usually accomplished via specialized protein complexes, which provide a polar transmembrane pore. Exceptions to this include bacterial toxins, which insert into and cross the lipid bilayer itself. We are studying the mechanism by which large antibacterial proteins enter Escherichia coli via specific outer membrane proteins. Here we describe the use of neutron scattering to investigate the interaction of colicin N with its outer membrane receptor protein OmpF. The positions of lipids, colicin N, and OmpF were separately resolved within complex structures by the use of selective deuteration. Neutron reflectivity showed, in real time, that OmpF mediates the insertion of colicin N into lipid monolayers. Here, this data were complemented by Brewster Angle Microscopy images, which showed a lateral association of OmpF in the presence of colicin N. Small angle neutron scattering experiments then defined the three-dimensional structure of the colicin N-OmpF complex. This revealed that colicin N unfolds and binds to the OmpF-lipid interface. The implications of this unfolding step for colicin translocation across membranes are discussed.

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Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1032832

Journal Information:: Journal of Biological Chemistry, Vol. 287, Issue 1; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 49 works

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59 BASIC BIOLOGICAL SCIENCES
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CELL MEMBRANES
DEUTERATION
ESCHERICHIA COLI
LIPIDS
MEMBRANE PROTEINS
MEMBRANES
MICROSCOPY
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REFLECTIVITY
RESOLUTION
SCATTERING
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Title: Low Resolution Structure and Dynamics of a Colicin-Receptor Complex Determined by Neutron Scattering

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