5WO2

Chaperone Spy bound to Casein Fragment (Casein un-modeled)

Replaces:  5IOG

Summary for 5WO2

• Entry DOI: 10.2210/pdb5wo2/pdb
• Descriptor: Periplasmic chaperone Spy, IMIDAZOLE, ZINC ION, ... (5 entities in total)
• Functional Keywords: chaperone
• Biological source: Escherichia coli
• Cellular location: Periplasm : P77754
• Total number of polymer chains: 2
• Total formula weight: 24612.51

Authors

Horowitz, S.,Koldewey, P.,Martin, R.,Bardwell, J.C.A. (deposition date: 2017-08-01, release date: 2017-08-16, Last modification date: 2023-10-04)

Primary citation

Horowitz, S.,Salmon, L.,Koldewey, P.,Ahlstrom, L.S.,Martin, R.,Quan, S.,Afonine, P.V.,van den Bedem, H.,Wang, L.,Xu, Q.,Trievel, R.C.,Brooks, C.L.,Bardwell, J.C.
Visualizing chaperone-assisted protein folding.
Nat. Struct. Mol. Biol., 23:691-697, 2016

PubMed 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.

PubMed: 27239796
DOI: 10.1038/nsmb.3237

Experimental method

X-RAY DIFFRACTION (1.769 Å)