1SKY

CRYSTAL STRUCTURE OF THE NUCLEOTIDE FREE ALPHA3BETA3 SUB-COMPLEX OF F1-ATPASE FROM THE THERMOPHILIC BACILLUS PS3


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.20 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.222 

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This is version 1.4 of the entry. See complete history


Literature

The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer.

Shirakihara, Y.Leslie, A.G.Abrahams, J.P.Walker, J.E.Ueda, T.Sekimoto, Y.Kambara, M.Saika, K.Kagawa, Y.Yoshida, M.

(1997) Structure 5: 825-836

  • DOI: https://doi.org/10.1016/s0969-2126(97)00236-0
  • Primary Citation of Related Structures:  
    1SKY

  • PubMed Abstract: 

    F1-ATPase, an oligomeric assembly with subunit stoichiometry alpha 3 beta 3 gamma delta epsilon, is the catalytic component of the ATP synthase complex, which plays a central role in energy transduction in bacteria, chloroplasts and mitochondria. The crystal structure of bovine mitochondrial F1-ATPase displays a marked asymmetry in the conformation and nucleotide content of the catalytic beta subunits. The alpha 3 beta 3 subcomplex of F1-ATPase has been assembled from subunits of the moderately thermophilic Bacillus PS3 made in Escherichia coli, and the subcomplex is active but does not show the catalytic cooperativity of intact F1-ATPase. The structure of this subcomplex should provide new information on the conformational variability of F1-ATPase and may provide insights into the unusual catalytic mechanism employed by this enzyme.


  • Organizational Affiliation

    Department of Physics, Hyogo University of Education, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
F1-ATPASEA [auth B]502Bacillus sp. PS3Mutation(s): 0 
UniProt
Find proteins for P09219 (Bacillus sp. (strain PS3))
Explore P09219 
Go to UniProtKB:  P09219
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP09219
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
F1-ATPASEB [auth E]473Bacillus sp. PS3Mutation(s): 0 
UniProt
Find proteins for P07677 (Bacillus sp. (strain PS3))
Explore P07677 
Go to UniProtKB:  P07677
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07677
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.20 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.222 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 159.5α = 90
b = 159.5β = 90
c = 159.5γ = 90
Software Package:
Software NamePurpose
AMoREphasing
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
CCP4data scaling
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-03-04
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Source and taxonomy, Version format compliance
  • Version 1.3: 2014-03-12
    Changes: Other
  • Version 1.4: 2024-02-14
    Changes: Data collection, Database references, Derived calculations