6DYM

C-terminal condensation domain of Ebony

6DYM の概要

• エントリーDOI: 10.2210/pdb6dym/pdb
• 分子名称: Ebony, CALCIUM ION (3 entities in total)
• 機能のキーワード: nrps, condensation domain, peptide-bond formation, biosynthetic protein
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26031.58

構造登録者

Izore, T.,Tailhades, J.,Hansen, M.H.,Kaczmarski, J.A.,Jackson, C.J.,Cryle, M.J. (登録日: 2018-07-02, 公開日: 2019-01-30, 最終更新日: 2024-03-13)

主引用文献

Izore, T.,Tailhades, J.,Hansen, M.H.,Kaczmarski, J.A.,Jackson, C.J.,Cryle, M.J.
Drosophila melanogasternonribosomal peptide synthetase Ebony encodes an atypical condensation domain.
Proc. Natl. Acad. Sci. U.S.A., 116:2913-2918, 2019

PubMed Abstract: The protein Ebony from plays a central role in the regulation of histamine and dopamine in various tissues through condensation of these amines with β-alanine. Ebony is a rare example of a nonribosomal peptide synthetase (NRPS) from a higher eukaryote and contains a C-terminal sequence that does not correspond to any previously characterized NRPS domain. We have structurally characterized this C-terminal domain and have discovered that it adopts the aryl-alkylamine--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.

PubMed: 30705105
DOI: 10.1073/pnas.1811194116

実験手法

X-RAY DIFFRACTION (2.02 Å)