3KO1

Cystal structure of thermosome from Acidianus tengchongensis strain S5


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.283 
  • R-Value Work: 0.277 
  • R-Value Observed: 0.277 

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This is version 1.2 of the entry. See complete history


Literature

Crystal structure of group II chaperonin in the open state.

Huo, Y.Hu, Z.Zhang, K.Wang, L.Zhai, Y.Zhou, Q.Lander, G.Zhu, J.He, Y.Pang, X.Xu, W.Bartlam, M.Dong, Z.Sun, F.

(2010) Structure 18: 1270-1279

  • DOI: https://doi.org/10.1016/j.str.2010.07.009
  • Primary Citation of Related Structures:  
    3KO1

  • PubMed Abstract: 

    Thermosomes are group II chaperonins responsible for protein refolding in an ATP-dependent manner. Little is known regarding the conformational changes of thermosomes during their functional cycle due to a lack of high-resolution structure in the open state. Here, we report the first complete crystal structure of thermosome (rATcpnβ) in the open state from Acidianus tengchongensis. There is a ∼30° rotation of the apical and lid domains compared with the previous closed structure. Besides, the structure reveals a conspicuous hydrophobic patch in the lid domain, and residues locating in this patch are conserved across species. Both the closed and open forms of rATcpnβ were also reconstructed by electron microscopy (EM). Structural fitting revealed the detailed conformational change from the open to the closed state. Structural comparison as well as protease K digestion indicated only ATP binding without hydrolysis does not induce chamber closure of thermosome.


  • Organizational Affiliation

    National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chaperonin
A, B, C, D, E
A, B, C, D, E, F, G, H, I
553Acidianus tengchongensisMutation(s): 0 
UniProt
Find proteins for Q877H2 (Acidianus tengchongensis)
Explore Q877H2 
Go to UniProtKB:  Q877H2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ877H2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.283 
  • R-Value Work: 0.277 
  • R-Value Observed: 0.277 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 223.674α = 90
b = 283.042β = 133.9
c = 160.75γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
PHASERphasing
REFMACrefinement
CNSrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-11-03
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description