6EMW

Structure of S.aureus ClpC in complex with MecA


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 11.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control.

Carroni, M.Franke, K.B.Maurer, M.Jager, J.Hantke, I.Gloge, F.Linder, D.Gremer, S.Turgay, K.Bukau, B.Mogk, A.

(2017) Elife 6

  • DOI: https://doi.org/10.7554/eLife.30120
  • Primary Citation of Related Structures:  
    6EM8, 6EM9, 6EMW

  • PubMed 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 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.


  • Organizational Affiliation

    Swedish Cryo-EM Facility, Science for Life Laboratory Stockholm University, Solna, Sweden.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent Clp protease ATP-binding subunit82Staphylococcus aureusMutation(s): 0 
Gene Names: E1951_02375E1E62_02425FF957_02715
UniProt
Find proteins for Q2G0P5 (Staphylococcus aureus (strain NCTC 8325 / PS 47))
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Go to UniProtKB:  Q2G0P5
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UniProt GroupQ2G0P5
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent Clp protease ATP-binding subunit225Staphylococcus aureusMutation(s): 0 
Gene Names: E1949_02445E1952_02450E1E63_02625
UniProt
Find proteins for Q2G0P5 (Staphylococcus aureus (strain NCTC 8325 / PS 47))
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UniProt GroupQ2G0P5
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Class III stress response-related ATPase, AAA+ superfamily55Staphylococcus aureusMutation(s): 0 
Gene Names: clpCBN1321_130009
UniProt
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UniProt GroupQ2G0P5
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent Clp protease ATP-binding subunit ClpC145Staphylococcus aureusMutation(s): 0 
Gene Names: 
UniProt
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UniProt GroupQ2G0P5
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent Clp protease ATP-binding subunit ClpC181Staphylococcus aureus RF122Mutation(s): 0 
Gene Names: clpCSAB0475
UniProt
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UniProt GroupQ2YSD6
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
ATP-dependent Clp protease ATP-binding subunit ClpC157Staphylococcus aureus RF122Mutation(s): 0 
Gene Names: clpCSAB0475
UniProt
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
Adapter protein MecA90Staphylococcus aureusMutation(s): 0 
Gene Names: mecAERS140147_01863
UniProt
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UniProt GroupQ2G1U5
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 11.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2017-12-27
    Type: Initial release
  • Version 1.1: 2018-10-24
    Changes: Advisory, Data collection, Derived calculations
  • Version 1.2: 2019-09-25
    Changes: Advisory, Data collection, Database references, Source and taxonomy, Structure summary