1BGY

CYTOCHROME BC1 COMPLEX FROM BOVINE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.360 
  • R-Value Work: 0.320 

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This is version 1.3 of the entry. See complete history


Literature

Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.

Iwata, S.Lee, J.W.Okada, K.Lee, J.K.Iwata, M.Rasmussen, B.Link, T.A.Ramaswamy, S.Jap, B.K.

(1998) Science 281: 64-71

  • DOI: https://doi.org/10.1126/science.281.5373.64
  • Primary Citation of Related Structures:  
    1BE3, 1BGY

  • PubMed Abstract: 

    Mitochondrial cytochrome bc1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. Refined crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme. The "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme. The mitochondrial targeting presequence of the "Rieske" protein (subunit 9) is lodged between the two "core" subunits at the matrix side of the complex. These "core" subunits are related to the matrix processing peptidase, and the structure unveils how mitochondrial targeting presequences are recognized.


  • Organizational Affiliation

    Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720, USA. iwata@xray.bmc.uu.se


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXA,
L [auth M]
446Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXB,
M [auth N]
439Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXC,
N [auth O]
379Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXD,
O [auth P]
241Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXE,
P [auth Q]
196Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXF,
Q [auth R]
110Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXG,
R [auth S]
81Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
UniProt
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXH,
S [auth T]
78Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXI,
T [auth U]
78Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXJ,
U [auth V]
62Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
CYTOCHROME BC1 COMPLEXK,
V [auth W]
56Bos taurusMutation(s): 0 
EC: 1.10.2.2
Membrane Entity: Yes 
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Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.360 
  • R-Value Work: 0.320 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 130.11α = 90
b = 130.11β = 90
c = 720.94γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
REFMACrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-01-06
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-08-02
    Changes: Database references, Derived calculations, Refinement description