2A1T

Structure of the human MCAD:ETF E165betaA complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.269 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.203 

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This is version 1.5 of the entry. See complete history


Literature

Stabilization of Non-productive Conformations Underpins Rapid Electron Transfer to Electron-transferring Flavoprotein

Toogood, H.S.van Thiel, A.Scrutton, N.S.Leys, D.

(2005) J Biol Chem 280: 30361-30366

  • DOI: https://doi.org/10.1074/jbc.M505562200
  • Primary Citation of Related Structures:  
    2A1T, 2A1U

  • PubMed Abstract: 

    Crystal structures of protein complexes with electron-transferring flavoprotein (ETF) have revealed a dual protein-protein interface with one region serving as anchor while the ETF FAD domain samples available space within the complex. We show that mutation of the conserved Glu-165beta in human ETF leads to drastically modulated rates of interprotein electron transfer with both medium chain acyl-CoA dehydrogenase and dimethylglycine dehydrogenase. The crystal structure of free E165betaA ETF is essentially identical to that of wild-type ETF, but the crystal structure of the E165betaA ETF.medium chain acyl-CoA dehydrogenase complex reveals clear electron density for the FAD domain in a position optimal for fast interprotein electron transfer. Based on our observations, we present a dynamic multistate model for conformational sampling that for the wild-type ETF. medium chain acyl-CoA dehydrogenase complex involves random motion between three distinct positions for the ETF FAD domain. ETF Glu-165beta plays a key role in stabilizing positions incompatible with fast interprotein electron transfer, thus ensuring high rates of complex dissociation.


  • Organizational Affiliation

    Department of Biochemistry, University of Leicester, Henry Wellcome Building, Lancaster Road, LE1 7RH, Leicester United Kingdom.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Acyl-CoA dehydrogenase, medium-chain specific, mitochondrial precursor
A, B, C, D
421Homo sapiensMutation(s): 0 
EC: 1.3.99.3
UniProt & NIH Common Fund Data Resources
Find proteins for P11310 (Homo sapiens)
Explore P11310 
Go to UniProtKB:  P11310
PHAROS:  P11310
GTEx:  ENSG00000117054 
Entity Groups  
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UniProt GroupP11310
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Electron transfer flavoprotein alpha-subunit, mitochondrial precursorE [auth R]333Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P13804 (Homo sapiens)
Explore P13804 
Go to UniProtKB:  P13804
PHAROS:  P13804
GTEx:  ENSG00000140374 
Entity Groups  
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UniProt GroupP13804
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Electron transfer flavoprotein beta-subunitF [auth S]255Homo sapiensMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P38117 (Homo sapiens)
Explore P38117 
Go to UniProtKB:  P38117
PHAROS:  P38117
GTEx:  ENSG00000105379 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP38117
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.269 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.203 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 94.184α = 90
b = 100.659β = 90
c = 244.384γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
AMoREphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-07-05
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-10-03
    Changes: Data collection
  • Version 1.4: 2021-11-10
    Changes: Database references, Derived calculations
  • Version 1.5: 2023-10-25
    Changes: Data collection, Refinement description