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 language | English |
|---|---|
| Pages (from-to) | 11287-11293 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 288 |
| Issue number | 16 |
| DOIs | |
| State | Published - 19 Apr 2013 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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