2Z51

Crystal structure of Arabidopsis CnfU involved in iron-sulfur cluster biosynthesis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.35 Å
  • R-Value Free: 0.173 
  • R-Value Work: 0.135 
  • R-Value Observed: 0.137 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural Analysis of Arabidopsis CnfU Protein: An Iron-Sulfur Cluster Biosynthetic Scaffold in Chloroplasts.

Yabe, T.Yamashita, E.Kikuchi, A.Morimoto, K.Nakagawa, A.Tsukihara, T.Nakai, M.

(2008) J Mol Biol 

  • DOI: https://doi.org/10.1016/j.jmb.2008.05.072
  • Primary Citation of Related Structures:  
    2Z51

  • PubMed Abstract: 

    CnfU, a key iron-sulfur (Fe-S) cluster biosynthetic scaffold that is required for biogenesis of ferredoxin and photosystem I in chloroplasts, consists of two tandemly repeated domains in which only the N-terminal domain contains a conserved CXXC motif. We have determined the crystal structure of the metal-free dimer of AtCnfU-V from Arabidopsis thaliana at 1.35 A resolution. The N-terminal domains of the two monomers are linked together through two intermolecular disulfide bonds between the CXXC motifs. At the dimer interface, a total of four cysteine sulfur atoms provide a Fe-S cluster assembly site surrounded by uncharged but hydrophilic structurally mobile segments. The C-terminal domain of one monomer interacts with the N-terminal domain of the opposing monomer and thereby stabilizes dimer formation. Furthermore, Fe K-edge X-ray absorption spectroscopic analysis of the holo-CnfU dimer in solution suggests the presence of a typical [2Fe-2S]-type cluster coordinated by four thiolate ligands. Based on these data, a plausible model of the holo-AtCnfU-V dimer containing a surface-exposed [2Fe-2S] cluster assembled in the dimer interface was deduced. We propose that such a structural framework is important for CnfU to function as a Fe-S cluster biosynthetic scaffold.


  • Organizational Affiliation

    Laboratory of Regulation of Biological Reactions, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita 565-0871, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NifU-like protein 2, chloroplast154Arabidopsis thalianaMutation(s): 0 
Gene Names: NIFU2CNFU2NFU2
UniProt
Find proteins for Q93W20 (Arabidopsis thaliana)
Explore Q93W20 
Go to UniProtKB:  Q93W20
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ93W20
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.35 Å
  • R-Value Free: 0.173 
  • R-Value Work: 0.135 
  • R-Value Observed: 0.137 
  • Space Group: P 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.546α = 90
b = 57.394β = 90
c = 61.303γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-07-15
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2018-06-27
    Changes: Data collection, Database references
  • Version 1.3: 2024-03-13
    Changes: Data collection, Database references, Derived calculations