Allosteric transitions direct protein tagging by PafA, the prokaryotic ubiquitin-like protein (Pup) ligase

Naomi Ofer, Nadav Forer, Maayan Korman, Marina Vishkautzan, Isam Khalaila, Eyal Gur

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

Background: The interaction of PafA, the prokaryotic ubiquitin-like ligase, with its protein substrates is poorly understood. Results: Measurements of PafA kinetics reveal cooperative substrate binding and experiments with engineered substrates suggest that PafA forms dimers. Conclusion: The PafA enzymatic mechanism involves allosteric transitions. Significance: PafA interaction with its target substrates is regulated at the enzyme level.

Original languageEnglish
Pages (from-to)11287-11293
Number of pages7
JournalJournal of Biological Chemistry
Volume288
Issue number16
DOIs
StatePublished - 19 Apr 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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