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Visualizing chaperone-assisted protein folding.

  • Author(s): Horowitz, Scott;
  • Salmon, Loïc;
  • Koldewey, Philipp;
  • Ahlstrom, Logan S;
  • Martin, Raoul;
  • Quan, Shu;
  • Afonine, Pavel V;
  • van den Bedem, Henry;
  • Wang, Lili;
  • Xu, Qingping;
  • Trievel, Raymond C;
  • Brooks, Charles L;
  • Bardwell, James CA
  • et al.

Published Web Location

https://doi.org/10.1038/nsmb.3237
Abstract

Challenges in determining the structures of heterogeneous and dynamic protein complexes have greatly hampered past efforts to obtain a mechanistic understanding of many important biological processes. One such process is chaperone-assisted protein folding. Obtaining structural ensembles of chaperone-substrate complexes would ultimately reveal how chaperones help proteins fold into their native state. To address this problem, we devised a new structural biology approach based on X-ray crystallography, termed residual electron and anomalous density (READ). READ enabled us to visualize even sparsely populated conformations of the substrate protein immunity protein 7 (Im7) in complex with the Escherichia coli chaperone Spy, and to capture a series of snapshots depicting the various folding states of Im7 bound to Spy. The ensemble shows that Spy-associated Im7 samples conformations ranging from unfolded to partially folded to native-like states and reveals how a substrate can explore its folding landscape while being bound to a chaperone.

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