2D5K

Crystal structure of Dps from Staphylococcus aureus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Nucleoid compaction by MrgA(Asp56Ala/Glu60Ala) does not contribute to staphylococcal cell survival against oxidative stress and phagocytic killing by macrophages

Ushijima, Y.Ohniwa, R.L.Maruyama, A.Saito, S.Tanaka, Y.Morikawa, K.

(2014) FEMS Microbiol Lett 360: 144-151

  • DOI: https://doi.org/10.1111/1574-6968.12598
  • Primary Citation of Related Structures:  
    2D5K

  • PubMed Abstract: 

    Staphylococcus aureus MrgA (encoded by mrgA) belongs to the Dps family of proteins, which play important roles in coping with various stresses. The staphylococcal mrgA gene is specifically expressed under oxidative stress conditions and is one of the most highly induced genes during phagocytic killing by macrophages. We previously reported that mrgA is essential for oxidative stress resistance, and can cause nucleoid compaction. However, whether nucleoid compaction by itself would contribute to oxidative stress resistance was hard to determine, because Dps family proteins generally have ferroxidase activity to prevent hydroxyl radical formation via the Fenton reaction. In this study, we resolved the crystal structure of MrgA and conducted mutation analysis of Asp56 and Glu60, which are located at the expected ferroxidase centre. In the strain expressing Asp56Ala/Glu60Ala MrgA (termed MrgA*), MrgA* retained dodecamer formation and nucleoid compaction ability. By contrast, the ferroxidase activity of MrgA* decreased by about half. Viability of the mrgA* strain was as low as the mrgA null mutant in oxidative stress and phagocytic killing assays. These results suggest that nucleoid compaction by itself is insufficient for oxidative stress resistance, and Asp56 and Glu60 constitute essential molecular sites in MrgA for oxidative stress resistance and survival against phagocytic killing.


  • Organizational Affiliation

    Graduate School of Comprehensive Human Science, University of Tsukuba, Tsukuba, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Dps family protein
A, B, C, D
156Staphylococcus aureus subsp. aureus COLMutation(s): 0 
EC: 4.2.1.52
UniProt
Find proteins for A0A0H2X069 (Staphylococcus aureus (strain COL))
Explore A0A0H2X069 
Go to UniProtKB:  A0A0H2X069
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H2X069
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 0.208 
  • R-Value Work: 0.190 
  • R-Value Observed: 0.190 
  • Space Group: P 3 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 143.381α = 90
b = 143.381β = 90
c = 88.288γ = 120
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-10-17
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Source and taxonomy, Version format compliance
  • Version 1.3: 2018-02-14
    Changes: Database references
  • Version 1.4: 2023-10-25
    Changes: Data collection, Database references, Derived calculations, Refinement description