| First Author | Izoré Thierry | Year | 2019 |
| Journal | Proc Natl Acad Sci U S A | Volume | 116 |
| Pages | 2913-2918 | PubMed ID | 30705105 |
| Abstract Text | N-acetyl transferase (AANAT) fold, which is unprecedented in NRPS biology. Through analysis of ligand-bound structures, activity assays, and binding measurements, we have determined how this atypical condensation domain is able to provide selectivity for both the carrier protein-bound amino acid and the amine substrates, a situation that remains unclear for standard condensation domains identified to date from NRPS assembly lines. These results demonstrate that the C terminus of Ebony encodes a eukaryotic example of an alternative type of NRPS condensation domain; they also illustrate how the catalytic components of such assembly lines are significantly more diverse than a minimal set of conserved functional domains. | Doi | 10.1073/pnas.1811194116 |
| Issue | 8 | Month | 02 |
