3J3S

Structural dynamics of the MecA-ClpC complex revealed by cryo-EM


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 1.5 of the entry. See complete history


Literature

Structural dynamics of the MecA-ClpC complex: a type II AAA+ protein unfolding machine.

Liu, J.Mei, Z.Li, N.Qi, Y.Xu, Y.Shi, Y.Wang, F.Lei, J.Gao, N.

(2013) J Biol Chem 288: 17597-17608

  • DOI: https://doi.org/10.1074/jbc.M113.458752
  • Primary Citation of Related Structures:  
    3J3R, 3J3S, 3J3T, 3J3U

  • PubMed Abstract: 

    The MecA-ClpC complex is a bacterial type II AAA(+) molecular machine responsible for regulated unfolding of substrates, such as transcription factors ComK and ComS, and targeting them to ClpP for degradation. The six subunits of the MecA-ClpC complex form a closed barrel-like structure, featured with three stacked rings and a hollow passage, where substrates are threaded and translocated through successive pores. Although the general concepts of how polypeptides are unfolded and translocated by internal pore loops of AAA(+) proteins have long been conceived, the detailed mechanistic model remains elusive. With cryoelectron microscopy, we captured four different structures of the MecA-ClpC complexes. These complexes differ in the nucleotide binding states of the two AAA(+) rings and therefore might presumably reflect distinctive, representative snapshots from a dynamic unfolding cycle of this hexameric complex. Structural analysis reveals that nucleotide binding and hydrolysis modulate the hexameric complex in a number of ways, including the opening of the N-terminal ring, the axial and radial positions of pore loops, the compactness of the C-terminal ring, as well as the relative rotation between the two nucleotide-binding domain rings. More importantly, our structural and biochemical data indicate there is an active allosteric communication between the two AAA(+) rings and suggest that concerted actions of the two AAA(+) rings are required for the efficiency of the substrate unfolding and translocation. These findings provide important mechanistic insights into the dynamic cycle of the MecA-ClpC unfoldase and especially lay a foundation toward the complete understanding of the structural dynamics of the general type II AAA(+) hexamers.


  • Organizational Affiliation

    Ministry of Education Key Laboratory of Protein Sciences, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Adapter protein MecA 1218Bacillus subtilis subsp. subtilis str. 168Mutation(s): 0 
Gene Names: mecABSU11520
UniProt
Find proteins for P37958 (Bacillus subtilis (strain 168))
Explore P37958 
Go to UniProtKB:  P37958
Entity Groups  
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UniProt GroupP37958
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Negative regulator of genetic competence ClpC/MecB810Bacillus subtilis subsp. subtilis str. 168Mutation(s): 1 
Gene Names: clpCmecBBSU00860
UniProt
Find proteins for P37571 (Bacillus subtilis (strain 168))
Explore P37571 
Go to UniProtKB:  P37571
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP37571
Sequence Annotations
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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 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONSPIDER

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-05-15
    Type: Initial release
  • Version 1.1: 2013-08-28
    Changes: Database references
  • Version 1.2: 2014-10-22
    Changes: Other
  • Version 1.3: 2015-01-21
    Changes: Other
  • Version 1.4: 2019-12-18
    Changes: Data collection, Database references
  • Version 1.5: 2024-03-20
    Changes: Data collection, Database references, Refinement description