3QO6

Crystal structure analysis of the plant protease Deg1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.228 

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This is version 1.3 of the entry. See complete history


Literature

Structural adaptation of the plant protease Deg1 to repair photosystem II during light exposure.

Kley, J.Schmidt, B.Boyanov, B.Stolt-Bergner, P.C.Kirk, R.Ehrmann, M.Knopf, R.R.Naveh, L.Adam, Z.Clausen, T.

(2011) Nat Struct Mol Biol 18: 728-731

  • DOI: https://doi.org/10.1038/nsmb.2055
  • Primary Citation of Related Structures:  
    3QO6

  • PubMed Abstract: 

    Deg1 is a chloroplastic protease involved in maintaining the photosynthetic machinery. Structural and biochemical analyses reveal that the inactive Deg1 monomer is transformed into the proteolytically active hexamer at acidic pH. The change in pH is sensed by His244, which upon protonation, repositions a specific helix to trigger oligomerization. This system ensures selective activation of Deg1 during daylight, when acidification of the thylakoid lumen occurs and photosynthetic proteins are damaged.


  • Organizational Affiliation

    Research Institute of Molecular Pathology (IMP), Vienna, Austria.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protease Do-like 1, chloroplastic
A, B, C
348Arabidopsis thalianaMutation(s): 0 
Gene Names: At3g27925Deg1DEGPDEGP1K16N12.18
EC: 3.4.21
UniProt
Find proteins for O22609 (Arabidopsis thaliana)
Explore O22609 
Go to UniProtKB:  O22609
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO22609
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
peptide7unidentifiedMutation(s): 0 
Sequence Annotations
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
peptide
E, H, I
4unidentifiedMutation(s): 0 
Sequence Annotations
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  • Reference Sequence

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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
peptide5unidentifiedMutation(s): 0 
Sequence Annotations
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  • Reference Sequence

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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
peptide3unidentifiedMutation(s): 0 
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.50 Å
  • R-Value Free: 0.268 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.228 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 126.135α = 90
b = 126.135β = 90
c = 328.303γ = 120
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
CNSrefinement
PDB_EXTRACTdata extraction
ADSCdata collection

Structure Validation

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Entry History 

Deposition Data

  • Released Date: 2011-05-04 
  • Deposition Author(s): Clausen, T.

Revision History  (Full details and data files)

  • Version 1.0: 2011-05-04
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2012-09-05
    Changes: Derived calculations
  • Version 1.3: 2023-09-13
    Changes: Data collection, Database references, Derived calculations, Refinement description