5B3P

Nqo5 of the trypsin-resistant fragment (1-134) in P212121 form

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.209 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.172 

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This is version 1.2 of the entry. See complete history. 


Literature

Characterization of the Nqo5 subunit of bacterial complex I in the isolated state

Hanazono, Y., Takeda, K., Miki, K.

(2016) FEBS Open Bio 6: 687-695

  • DOI: https://doi.org/10.1002/2211-5463.12070
  • Primary Citation of Related Structures:  
    5B3P, 5B3Q

  • PubMed Abstract: 

    The subunits that comprise bacterial complex I (NADH:ubiquinone oxidoreductase) are also found in more complicated mitochondrial enzymes in eukaryotic organisms. Although the Nqo5 subunit is one of these conserved components and important for the formation of complex, it has been little studied. Here, we report structure analyses of isolated Nqo5 from Thermus thermophilus. Biochemical studies indicated that the C-terminal region following the 30-Kd subunit motif is disordered in the isolated state, while the remaining portion is already folded. Crystallographic studies of a trypsin-resistant fragment revealed detailed structural differences in the folded domain between the isolated and complexed states.

    • Organizational Affiliation: 

    Department of Chemistry Graduate School of Science Kyoto University Sakyo-ku Kyoto Japan.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NADH-quinone oxidoreductase subunit 5134Thermus thermophilus HB8Mutation(s): 0 
Gene Names: nqo5, TTHA0086
EC: 1.6.5.11
UniProt
Find proteins for Q56219 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q56219 
Go to UniProtKB:  Q56219
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ56219
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.209 
  • R-Value Work: 0.170 
  • R-Value Observed: 0.172 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 41.264α = 90
b = 42.185β = 90
c = 70.095γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
AutoSolphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-07-27
    Type: Initial release
  • Version 1.1: 2020-02-26
    Changes: Data collection, Derived calculations
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references, Derived calculations