5IOE: Chaperone Spy H96l Bound To Im7 L18a L19a L37a (im7 Un-modeled)

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.
PDB ID: 5IOEDownload
MMDB ID: 139781
PDB Deposition Date: 2016/3/8
Updated in MMDB: 2016/07
Experimental Method:
x-ray diffraction
Resolution: 1.87  Å
Source Organism:

*This structure record is obsolete.

Molecular Components in 5IOE
Label Count Molecule
Proteins (2 molecules)
Spheroplast Protein Y
Molecule annotation
Chemicals (38 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB