1E18 | pdb_00001e18

TUNGSTEN-SUSBSTITUTED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 
    0.192 (Depositor) 
  • R-Value Work: 
    0.142 (Depositor) 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Dimethylsulfoxide Reductase: An Enzyme Capable of Catalysis with Either Molybdenum or Tungsten at the Active Site

Stewart, L.J., Bailey, S., Bennett, B., Charnock, J.M., Garner, C.D., Mcalpine, A.S.

(2000) J Mol Biology 299: 593

  • DOI: https://doi.org/10.1006/jmbi.2000.3702
  • Primary Citation of Related Structures:  
    1E18

  • PubMed Abstract: 

    DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will bind tungsten. Protein crystallography has shown that tungsten in W-DMSOR is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOR. These conclusions are consistent with W L(III)-edge X-ray absorption, EPR and UV/visible spectroscopic data. W-DMSOR is significantly more active than Mo-DMSOR in catalysing the reduction of DMSO but, in contrast to the latter, shows no significant ability to catalyse the oxidation of DMS.

    • Organizational Affiliation: 

    CLRC Daresbury Laboratory, Daresbury, Warrington, Cheshire, WA4 4AD, UK.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
DMSO REDUCTASE.823Rhodobacter capsulatusMutation(s): 0 
EC: 1.7.2.3 (UniProt), 1.8.5.3 (UniProt)
UniProt
Find proteins for Q52675 (Rhodobacter capsulatus)
Explore Q52675 
Go to UniProtKB:  Q52675
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ52675
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free:  0.192 (Depositor) 
  • R-Value Work:  0.142 (Depositor) 
Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 80.92α = 90
b = 80.92β = 90
c = 229.78γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-06-11
    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: 2024-05-08
    Changes: Data collection, Database references, Derived calculations