|Entry||Database: EMDB / ID: 3895|
|Title||S.aureus ClpC resting state, asymmetric map|
|Sample||Resting-state oligomeric complex of S. aureus ClpC|
|Function/homology||UVR domain profile. / UVR domain / ClpA/B, conserved site 2 / Chaperonins clpA/B signature 2. / UvrB/uvrC motif / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / Clp, N-terminal / Clp, N-terminal domain superfamily / ClpA/B family ...UVR domain profile. / UVR domain / ClpA/B, conserved site 2 / Chaperonins clpA/B signature 2. / UvrB/uvrC motif / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / Clp, N-terminal / Clp, N-terminal domain superfamily / ClpA/B family / protein metabolic process / Clp ATPase, C-terminal / Clp amino terminal domain, pathogenicity island component / AAA domain (Cdc48 subfamily) / C-terminal, D2-small domain, of ClpB protein / ATPase, AAA-type, core / ATPase family associated with various cellular activities (AAA) / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase / ATP binding / ATP-dependent Clp protease ATP-binding subunit ClpC|
Function and homology information
|Source||Staphylococcus aureus / / bacteria|
|Method||Cryo EM / single particle reconstruction / 8.4 Å resolution|
|Authors||Carroni M / Mogk A|
|Citation||Journal: Elife / Year: 2017|
Title: Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control.
Authors: Marta Carroni / Kamila B Franke / Michael Maurer / Jasmin Jäger / Ingo Hantke / Felix Gloge / Daniela Linder / Sebastian Gremer / Kürşad Turgay / Bernd Bukau / Axel Mogk
Abstract: Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and ...Ring-forming AAA+ chaperones exert ATP-fueled substrate unfolding by threading through a central pore. This activity is potentially harmful requiring mechanisms for tight repression and substrate-specific activation. The AAA+ chaperone ClpC with the peptidase ClpP forms a bacterial protease essential to virulence and stress resistance. The adaptor MecA activates ClpC by targeting substrates and stimulating ClpC ATPase activity. We show how ClpC is repressed in its ground state by determining ClpC cryo-EM structures with and without MecA. ClpC forms large two-helical assemblies that associate via head-to-head contacts between coiled-coil middle domains (MDs). MecA converts this resting state to an active planar ring structure by binding to MD interaction sites. Loss of ClpC repression in MD mutants causes constitutive activation and severe cellular toxicity. These findings unravel an unexpected regulatory concept executed by coiled-coil MDs to tightly control AAA+ chaperone activity.
|Validation Report||PDB-ID: 6em9|
SummaryFull reportAbout validation report
|Date||Deposition: Oct 1, 2017 / Header (metadata) release: Dec 27, 2017 / Map release: Dec 27, 2017 / Last update: Dec 27, 2017|
Downloads & links
|File||emd_3895.map.gz (map file in CCP4 format, 108001 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 1.34 Å|
CCP4 map header:
|File||emd_3895_msk_1.map ( map file in CCP4 format, 108001 KB )|
|Projections & Slices|
|Data type||Image stored as Reals|
|Space group number||1|
-Entire Resting-state oligomeric complex of S. aureus ClpC
|Entire||Name: Resting-state oligomeric complex of S. aureus ClpC / Number of components: 2|
|Mass||Experimental: 900 kDa|
-Component #1: protein, Resting-state oligomeric complex of S. aureus ClpC
|Protein||Name: Resting-state oligomeric complex of S. aureus ClpC / Recombinant expression: No|
|Mass||Experimental: 900 kDa|
|Source||Species: Staphylococcus aureus / / bacteria / Strain: bovine RF122 / ET3-1|
|Source (engineered)||Expression System: Escherichia coli / / bacteria /|
-Component #2: protein, ATP-dependent Clp protease ATP-binding subunit ClpC
|Protein||Name: ATP-dependent Clp protease ATP-binding subunit ClpC / Recombinant expression: No|
|Mass||Theoretical: 91.200375 kDa|
|Source (engineered)||Expression System: Staphylococcus aureus (strain bovine rf122 / et3-1) / / bacteria|
Strain: bovine RF122 / ET3-1
|Specimen||Specimen state: particle / Method: Cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 297 K / Humidity: 100 %|
-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: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD / Defocus: 1000 - 3000 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 40000|
|3D reconstruction||Software: RELION / Resolution: 8.4 Å / Resolution method: FSC 0.143 CUT-OFF|
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