1SJ1

The 1.5 A Resolution Crystal Structure of [Fe3S4]-Ferredoxin from the hyperthermophilic Archaeon Pyrococcus furiosus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.195 

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This is version 1.2 of the entry. See complete history


Literature

The 1.5 A Resolution Crystal Structure of [Fe3S4]-Ferredoxin from the Hyperthermophilic Archaeon Pyrococcus furiosus

Nielsen, M.S.Harris, P.Ooi, B.L.Christensen, H.E.M.

(2004) Biochemistry 43: 5188-5194

  • DOI: https://doi.org/10.1021/bi049942x
  • Primary Citation of Related Structures:  
    1SIZ, 1SJ1

  • PubMed Abstract: 

    The structure of [Fe(3)S(4)]-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus has been determined to 1.5 A resolution from a crystal belonging to space group P2(1) with two molecules in the asymmetric unit. The structure has been solved with molecular replacement by use of the ferredoxin from Thermotoga maritima. The fold is similar to that of related monocluster ferredoxins and contains two double-stranded antiparallel beta-sheets and two alpha-helices. The hydrophobic interaction between Trp2 and Tyr46 is confirmed, linking the C-terminus to the longer alpha-helix. The structure contains a double-conformation disulfide bond existing in a left-handed and a right-handed spiral conformation. The crystal packing reveals a beta-sheet interaction, which supports the suggestion that P. furiosus ferredoxin is a functional dimer. The extraordinary thermostability of P. furiosus ferredoxin is further discussed.


  • Organizational Affiliation

    Department of Chemistry, Building 207, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ferredoxin
A, B
66Pyrococcus furiosusMutation(s): 0 
Gene Names: FDXAPF1909
UniProt
Find proteins for P29603 (Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1))
Explore P29603 
Go to UniProtKB:  P29603
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29603
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.50 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.194 
  • R-Value Observed: 0.195 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 31.23α = 90
b = 47.511β = 103.86
c = 52.029γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
CCP4data scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-05-25
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance