5AWF

Crystal structure of SufB-SufC-SufD complex from Escherichia coli


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.96 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.188 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis

Hirabayashi, K.Yuda, E.Tanaka, N.Katayama, S.Iwasaki, K.Matsumoto, T.Kurisu, G.Outten, F.W.Fukuyama, K.Takahashi, Y.Wada, K.

(2015) J Biol Chem 290: 29717-29731

  • DOI: https://doi.org/10.1074/jbc.M115.680934
  • Primary Citation of Related Structures:  
    5AWF, 5AWG

  • PubMed Abstract: 

    ATP-binding cassette (ABC)-type ATPases are chemomechanical engines involved in diverse biological pathways. Recent genomic information reveals that ABC ATPase domains/subunits act not only in ABC transporters and structural maintenance of chromosome proteins, but also in iron-sulfur (Fe-S) cluster biogenesis. A novel type of ABC protein, the SufBCD complex, functions in the biosynthesis of nascent Fe-S clusters in almost all Eubacteria and Archaea, as well as eukaryotic chloroplasts. In this study, we determined the first crystal structure of the Escherichia coli SufBCD complex, which exhibits the common architecture of ABC proteins: two ABC ATPase components (SufC) with function-specific components (SufB-SufD protomers). Biochemical and physiological analyses based on this structure provided critical insights into Fe-S cluster assembly and revealed a dynamic conformational change driven by ABC ATPase activity. We propose a molecular mechanism for the biogenesis of the Fe-S cluster in the SufBCD complex.


  • Organizational Affiliation

    From the Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka 560-0043, Japan, the Organization for Promotion of Tenure Track, University of Miyazaki, Miyazaki 889-1692, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FeS cluster assembly protein SufB
A, E
495Escherichia coli K-12Mutation(s): 0 
Gene Names: sufBynhEb1683JW5273
UniProt
Find proteins for P77522 (Escherichia coli (strain K12))
Explore P77522 
Go to UniProtKB:  P77522
Entity Groups  
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UniProt GroupP77522
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
FeS cluster assembly protein SufD
B, F
423Escherichia coli K-12Mutation(s): 0 
Gene Names: sufDynhCb1681JW1671
UniProt
Find proteins for P77689 (Escherichia coli (strain K12))
Explore P77689 
Go to UniProtKB:  P77689
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UniProt GroupP77689
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Probable ATP-dependent transporter SufC
C, D, G, H
248Escherichia coli K-12Mutation(s): 0 
Gene Names: sufCynhDb1682JW1672
UniProt
Find proteins for P77499 (Escherichia coli (strain K12))
Explore P77499 
Go to UniProtKB:  P77499
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP77499
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.96 Å
  • R-Value Free: 0.226 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.188 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 119.475α = 90
b = 139.556β = 113.1
c = 124.684γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
HKL-2000data scaling
PHENIXphasing
Cootmodel building
HKL-2000data reduction

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-11-11
    Type: Initial release
  • Version 1.1: 2016-02-17
    Changes: Database references
  • Version 1.2: 2020-02-26
    Changes: Data collection, Database references, Derived calculations
  • Version 1.3: 2021-08-11
    Changes: Database references, Structure summary
  • Version 1.4: 2024-05-29
    Changes: Data collection