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Nat Struct Mol Biol. 2016 Jul;23(7):691-7. doi: 10.1038/nsmb.3237. Epub 2016 May 30.

Visualizing chaperone-assisted protein folding.

Author information

1
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA.
2
Howard Hughes Medical Institute, Ann Arbor, Michigan, USA.
3
Department of Chemistry and Biophysics Program, University of Michigan, Ann Arbor, Michigan, USA.
4
State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai Collaborative Innovation Center for Biomanufacturing, Shanghai, China.
5
Lawrence Berkeley National Laboratory, Berkeley, California, USA.
6
Division of Biosciences, SLAC National Accelerator Laboratory, Stanford University, Stanford, California, USA.
7
Joint Center for Structural Genomics, Stanford Synchrotron Radiation Lightsource, SLAC National Laboratory, Menlo Park, California, USA.
8
Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.

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.

PMID:
27239796
PMCID:
PMC4937829
DOI:
10.1038/nsmb.3237
[Indexed for MEDLINE]
Free PMC Article

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