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Visualizing chaperone-assisted protein folding.

Nat. Struct. Mol. Biol.2016 Jul;23(7):691-7. Epub 2016 May 30
Scott Horowitz 1 , Loïc Salmon 1 , Philipp Koldewey 1 , Logan S Ahlstrom 2 , Raoul Martin 1 , Shu Quan 3 , Pavel V Afonine 4 , Henry van den Bedem 5 , Lili Wang 1 , Qingping Xu 6 , Raymond C Trievel 7 , Charles L Brooks 2 , James C A Bardwell 1
Scott Horowitz 1 , Loïc Salmon 1 , Philipp Koldewey 1 , Logan S Ahlstrom 2 , Raoul Martin 1 , Shu Quan 3 , Pavel V Afonine 4 , Henry van den Bedem 5 , Lili Wang 1 , Qingping Xu 6 , Raymond C Trievel 7 , Charles L Brooks 2 , James C A Bardwell 1
+ et al

[No authors listed]

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

摘要

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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