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Structure paper

TitleStructural basis for the recognition and ubiquitylation of type-2 N-degron substrate by PRT1 plant N-recognin.
Journal, issue, pagesNat Commun, Vol. 16, Page 7817-7817, Year 2025
Publish dateMay 9, 2024 (structure data deposition date)
AuthorsYang, W.S. / Kim, S.H. / Kim, M. / Shin, H. / Lee, J. / Sandmann, A. / Park, O.K. / Dissmeyer, N. / Song, H.K.
External linksNat Commun / PubMed:40841552
MethodsX-ray diffraction
Resolution1.673 - 2.785 Å
Structure data

PDB-8zg8:
ZZ-domain of the Arabidopsis thaliana E3 ubiquitin-protein ligase PRT1
Method: X-RAY DIFFRACTION / Resolution: 1.744 Å

PDB-8zg9:
Y-degron fused ZZ-domain of the Arabidopsis thaliana E3 ubiquitin-protein ligase PRT1
Method: X-RAY DIFFRACTION / Resolution: 1.673 Å

PDB-8zga:
F-degron fused ZZ-domain of the Arabidopsis thaliana E3 ubiquitin-protein ligase PRT1
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-8zgb:
W-degron fused ZZ-domain of the Arabidopsis thaliana E3 ubiquitin-protein ligase PRT1
Method: X-RAY DIFFRACTION / Resolution: 2.785 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

Source
  • arabidopsis thaliana (thale cress)
KeywordsLIGASE / Apo / ZZ-domain / Arabidopsis thaliana / PRT1 / E3-ubiquitin ligase / complex

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