|Entry||Database: EMDB / Id: 4293|
|Source||Homo sapiens (human)|
|Method||single particle reconstruction / cryo EM / Resolution: 15 Å|
|Authors||Quintana-Gallardo L / Martin-Benito J / Valpuesta JM|
|Citation||Journal: Sci Rep / Year: 2019|
Title: The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism.
P-authors: Lucía Quintana-Gallardo / Jaime Martín-Benito / Miguel Marcilla / Guadalupe Espadas / Eduard Sabidó / José María Valpuesta /
Abstract: Some molecular chaperones are involved not only in assisting the folding of proteins but also, given appropriate conditions, in their degradation. This is the case for Hsp70 and Hsp90 which, in ...Some molecular chaperones are involved not only in assisting the folding of proteins but also, given appropriate conditions, in their degradation. This is the case for Hsp70 and Hsp90 which, in concert with the cochaperone CHIP, direct their bound substrate to degradation through ubiquitination. We generated complexes between the chaperones (Hsp70 or Hsp90), the cochaperone CHIP and, as substrate, a p53 variant containing the GST protein (p53-TMGST). Both ternary complexes (Hsp70:p53-TMGST:CHIP and Hsp90:p53-TMGST:CHIP) ubiquitinated the substrate at a higher efficiency than in the absence of the chaperones. The 3D structures of the two complexes, obtained using a combination of cryoelectron microscopy and crosslinking mass spectrometry, showed the substrate located between the chaperone and the cochaperone, suggesting a ubiquitination mechanism in which the chaperone-bound substrate is presented to CHIP. These complexes are inherently flexible, which is important for the ubiquitination process.
|Date||Deposition: Feb 7, 2018 / Header (metadata) release: Mar 14, 2018 / Map release: Mar 20, 2019 / Last update: Mar 20, 2019|
|Structure viewer||EM map: |
|File||emd_4293.map.gz (map file in CCP4 format, 32001 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.8 Å|
CCP4 map header:
|Entire||Name: Hsp70:p53-TMGST:CHIP / Number of components: 1|
-Component #1: protein, Hsp70:p53-TMGST:CHIP
|Protein||Name: Hsp70:p53-TMGST:CHIP / Recombinant expression: No|
|Mass||Theoretical: 200 MDa|
|Source||Species: Homo sapiens (human)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Ph: 7.4|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 30 e/Å2 / Illumination mode: SPOT SCAN|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 QUANTUM (4k x 4k)|
|Processing||Method: single particle reconstruction / Number of projections: 25000|
|3D reconstruction||Resolution: 15 Å / Resolution method: FSC 0.33 CUT-OFF|
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