Structural mapping of a chaperone-substrate interaction surface.
NMR spectroscopy is used to detect site-specific intermolecular short-range contacts in a membrane-protein-chaperone complex. This is achieved by an "orthogonal" isotope-labeling scheme that permits the unambiguous detection of intermolecular NOEs between the well-folded chaperone and the unfolded substrate ensemble. The residues involved in these contacts are part of the chaperone-substrate contact interface. The approach is demonstrated for the 70 kDa bacterial Skp-tOmpA complex.
Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel (Switzerland).
Morgane
M
Callon
Björn M
BM
Burmann
Sebastian
S
Hiller
D001665:Binding Sites; D009682:Magnetic Resonance Spectroscopy; D018832:Molecular Chaperones / Q000737:chemistry*; D011487:Protein Conformation
D018832:Molecular Chaperones
NMR spectroscopy; chaperone proteins; membrane proteins; protein ensembles; protein-protein interactions