|Entry||Database: EMDB / ID: 8318|
|Title||Mutant E. coli GroEL (C-terminal truncated) bound with PepQ|
|Map data||mutant E. coli GroEL (C-terminal truncated) bound with PepQ|
|Sample||Tetradecamer complex of C-terminal truncated mutant E. coli GroEL bound with PepQ:|
GroEL / PepQ
|Function / homology||GroEL-like equatorial domain superfamily / Creatinase/Aminopeptidase P/Spt16, N-terminal / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / Xaa-Pro dipeptidase / Chaperonin Cpn60, conserved site / Chaperonin Cpn60/TCP-1 family / Chaperonin Cpn60 / Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site / Peptidase M24 ...GroEL-like equatorial domain superfamily / Creatinase/Aminopeptidase P/Spt16, N-terminal / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / Xaa-Pro dipeptidase / Chaperonin Cpn60, conserved site / Chaperonin Cpn60/TCP-1 family / Chaperonin Cpn60 / Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site / Peptidase M24 / Creatinase/aminopeptidase-like / TCP-1/cpn60 chaperonin family / Aminopeptidase P and proline dipeptidase signature. / Chaperonins cpn60 signature. / Metallopeptidase family M24 / phosphoric triester hydrolase activity / Xaa-Pro dipeptidase / proline dipeptidase activity / metallodipeptidase activity / GroEL-GroES complex / dipeptidase activity / 'de novo' protein folding / peptide catabolic process / chaperone cofactor-dependent protein refolding / virion assembly / protein folding / response to radiation / unfolded protein binding / response to heat / manganese ion binding / protein refolding / ATPase activity / cell cycle / cell division / magnesium ion binding / membrane / ATP binding / identical protein binding / cytosol / 60 kDa chaperonin / Xaa-Pro dipeptidase|
Function and homology information
|Source||Escherichia coli (E. coli) / Escherichia (bacteria)|
|Method||single particle reconstruction / cryo EM / 8.3 Å resolution|
|Authors||Jiang M / Zhang J|
|Citation||Journal: Nat Commun / Year: 2017|
Title: GroEL actively stimulates folding of the endogenous substrate protein PepQ.
Authors: Jeremy Weaver / Mengqiu Jiang / Andrew Roth / Jason Puchalla / Junjie Zhang / Hays S Rye
|Date||Deposition: Aug 10, 2016 / Header (metadata) release: Oct 5, 2016 / Map release: Jul 12, 2017 / Last update: Jul 12, 2017|
|Structure viewer||EM map: |
Downloads & links
|File||emd_8318.map.gz (map file in CCP4 format, 2049 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 3.7 Å|
CCP4 map header:
-Entire Tetradecamer complex of C-terminal truncated mutant E. coli GroEL...
|Entire||Name: Tetradecamer complex of C-terminal truncated mutant E. coli GroEL bound with PepQ|
Number of components: 3
-Component #1: protein, Tetradecamer complex of C-terminal truncated mutant E. c...
|Protein||Name: Tetradecamer complex of C-terminal truncated mutant E. coli GroEL bound with PepQ|
Recombinant expression: No
|Source||Species: Escherichia coli (E. coli)|
|Source (engineered)||Expression System: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)|
-Component #2: protein, GroEL
|Protein||Name: GroEL / Recombinant expression: No|
|Source||Species: Escherichia coli (E. coli)|
-Component #3: protein, PepQ
|Protein||Name: PepQ / Recombinant expression: No|
|Source||Species: Escherichia (bacteria)|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Tecnai F20 / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI F20|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 19 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: single particle reconstruction / Number of projections: 26392|
|3D reconstruction||Resolution: 8.3 Å / Resolution method: FSC 0.143 CUT-OFF|
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