1EFR

BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.177 

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This is version 1.6 of the entry. See complete history


Literature

The Structure of Bovine F1-ATPase Complexed with the Peptide Antibiotic Efrapeptin.

Abrahams, J.P.Buchanan, S.K.Van Raaij, M.J.Fearnley, I.M.Leslie, A.G.Walker, J.E.

(1996) Proc Natl Acad Sci U S A 93: 9420

  • DOI: https://doi.org/10.1073/pnas.93.18.9420
  • Primary Citation of Related Structures:  
    1EFR

  • PubMed Abstract: 

    In the previously determined structure of mitochondrial F1-ATPase determined with crystals grown in the presence of adenylyl-imidodiphosphate (AMP-PNP) and ADP, the three catalytic beta-subunits have different conformations and nucleotide occupancies. AMP-PNP and ADP are bound to subunits beta TP and beta DP, respectively, and the third beta-subunit (beta E) has no bound nucleotide. The efrapeptins are a closely related family of modified linear peptides containing 15 amino acids that inhibit both ATP synthesis and hydrolysis by binding to the F1 catalytic domain of F1F0-ATP synthase. In crystals of F1-ATPase grown in the presence of both nucleotides and inhibitor, efrapeptin is bound to a unique site in the central cavity of the enzyme. Its binding is associated with small structural changes in side chains of F1-ATPase around the binding pocket. Efrapeptin makes hydrophobic contacts with the alpha-helical structure in the gamma-subunit, which traverses the cavity, and with subunit beta E and the two adjacent alpha-subunits. Two intermolecular hydrogen bonds could also form. Intramolecular hydrogen bonds probably help to stabilize efrapeptin's two domains (residues 1-6 and 9-15, respectively), which are connected by a flexible region (beta Ala-7 and Gly-8). Efrapeptin appears to inhibit F1-ATPase by blocking the conversion of subunit beta E to a nucleotide binding conformation, as would be required by an enzyme mechanism involving cyclic interconversion of catalytic sites.


  • Organizational Affiliation

    Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA
A, B, C
510Bos taurusMutation(s): 0 
Membrane Entity: Yes 
UniProt
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Go to UniProtKB:  P19483
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UniProt GroupP19483
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT BETA
D, E, F
482Bos taurusMutation(s): 0 
Membrane Entity: Yes 
UniProt
Find proteins for P00829 (Bos taurus)
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Go to UniProtKB:  P00829
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UniProt GroupP00829
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT GAMMA272Bos taurusMutation(s): 0 
Membrane Entity: Yes 
UniProt
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Go to UniProtKB:  P05631
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UniProt GroupP05631
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  • Reference Sequence

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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
EFRAPEPTIN CH [auth Q]17Tolypocladium inflatumMutation(s): 0 
Membrane Entity: Yes 
UniProt
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Explore P05631 
Go to UniProtKB:  P05631
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UniProt GroupP05631
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  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ANP
Query on ANP

Download Ideal Coordinates CCD File 
J [auth A],
L [auth B],
N [auth C],
R [auth F]
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
C10 H17 N6 O12 P3
PVKSNHVPLWYQGJ-KQYNXXCUSA-N
ADP
Query on ADP

Download Ideal Coordinates CCD File 
P [auth D]ADENOSINE-5'-DIPHOSPHATE
C10 H15 N5 O10 P2
XTWYTFMLZFPYCI-KQYNXXCUSA-N
MG
Query on MG

Download Ideal Coordinates CCD File 
I [auth A],
K [auth B],
M [auth C],
O [auth D],
Q [auth F]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
AIB
Query on AIB
H [auth Q]L-PEPTIDE LINKINGC4 H9 N O2ALA
Biologically Interesting Molecules (External Reference) 1 Unique
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.10 Å
  • R-Value Free: 0.220 
  • R-Value Work: 0.177 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 285.7α = 90
b = 107.4β = 90
c = 139.5γ = 90
Software Package:
Software NamePurpose
CCP4model building
TNTrefinement
MOSFLMdata reduction
CCP4data scaling
CCP4phasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1997-02-12
    Type: Initial release
  • Version 1.1: 2011-06-14
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2011-07-27
    Changes: Atomic model, Database references, Derived calculations, Non-polymer description, Structure summary
  • Version 1.4: 2012-12-12
    Changes: Other
  • Version 1.5: 2017-11-01
    Changes: Advisory, Derived calculations, Other
  • Version 1.6: 2023-08-09
    Changes: Advisory, Database references, Derived calculations, Refinement description