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Structural Mapping of a Chaperone–Substrate Interaction Surface

Authors


  • This work was supported by grants from the Swiss National Science Foundation (Grant PP00P3_128419) and the European Research Council (FP7 contract MOMP 281764) to S.H., and by a personal fellowship from the Werner-Siemens Foundation to M.C.

Abstract

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.

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