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TitleBacterial ligases reveal fundamental principles of polyubiquitin specificity.
Journal, issue, pagesMol. Cell, Vol. 83, Page 4538-4554.e4, Year 2023
Publish dateMay 9, 2023 (structure data deposition date)
AuthorsFranklin, T.G. / Brzovic, P.S. / Pruneda, J.N.
External linksMol. Cell / PubMed:38091999
MethodsX-ray diffraction
Resolution1.44 - 2.5 Å
Structure data

PDB-8st7:
Structure of E3 ligase VsHECT bound to ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 1.44 Å

PDB-8st8:
Structure of E3 ligase SopA bound to ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-8st9:
Structure of E3 ligase NleL bound to ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-AYE:
prop-2-en-1-amine

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • verrucomicrobiota (bacteria)
  • salmonella enterica subsp. enterica serovar typhimurium (bacteria)
  • escherichia coli o157:h7 str. sakai (bacteria)
KeywordsTRANSFERASE / E3 ubiquitin ligase / LIGASE

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