2CB2

Sulfur Oxygenase Reductase from Acidianus Ambivalens


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.210 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.183 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

X-Ray Structure of a Self-Compartmentalizing Sulfur Cycle Metalloenzyme

Urich, T.Gomes, C.M.Kletzin, A.Frazao, C.

(2006) Science 311: 996

  • DOI: https://doi.org/10.1126/science.1120306
  • Primary Citation of Related Structures:  
    2CB2

  • PubMed Abstract: 

    Numerous microorganisms oxidize sulfur for energy conservation and contribute to the global biogeochemical sulfur cycle. We have determined the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes an oxygen-dependent disproportionation of elemental sulfur. Twenty-four monomers form a large hollow sphere enclosing a positively charged nanocompartment. Apolar channels provide access for linear sulfur species. A cysteine persulfide and a low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitute the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction.


  • Organizational Affiliation

    Darmstadt University of Technology, Institute of Microbiology and Genetics, Schnittspahnstrasse 10, 64287 Darmstadt, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SULFUR OXYGENASE REDUCTASE
A, B, C, D, E
A, B, C, D, E, F
318Acidianus ambivalensMutation(s): 0 
UniProt
Find proteins for P29082 (Acidianus ambivalens)
Explore P29082 
Go to UniProtKB:  P29082
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29082
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.210 
  • R-Value Work: 0.183 
  • R-Value Observed: 0.183 
  • Space Group: I 4
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 162.15α = 90
b = 162.15β = 90
c = 154.93γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
SHELXDphasing
SOLVEphasing
ARP/wARPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-02-24
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-06-28
    Changes: Refinement description
  • Version 1.4: 2019-05-08
    Changes: Data collection, Derived calculations, Experimental preparation
  • Version 1.5: 2019-07-24
    Changes: Data collection