4Q84

Apo YcaO

4Q84 の概要

• エントリーDOI: 10.2210/pdb4q84/pdb
• 関連するPDBエントリー: 4q85 4q86
• 分子名称: Ribosomal protein S12 methylthiotransferase accessory factor YcaO, MERCURY (II) ION (3 entities in total)
• 機能のキーワード: ycao atp binding domain, protein binding
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 132206.58

構造登録者

Chekan, J.R.,Nair, S.K. (登録日: 2014-04-25, 公開日: 2014-08-13, 最終更新日: 2024-02-28)

主引用文献

Dunbar, K.L.,Chekan, J.R.,Cox, C.L.,Burkhart, B.J.,Nair, S.K.,Mitchell, D.A.
Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.
Nat.Chem.Biol., 10:823-829, 2014

PubMed Abstract: Despite intensive research, the cyclodehydratase responsible for azoline biogenesis in thiazole/oxazole-modified microcin (TOMM) natural products remains enigmatic. The collaboration of two proteins, C and D, is required for cyclodehydration. The C protein is homologous to E1 ubiquitin-activating enzymes, whereas the D protein is within the YcaO superfamily. Recent studies have demonstrated that TOMM YcaOs phosphorylate amide carbonyl oxygens to facilitate azoline formation. Here we report the X-ray crystal structure of an uncharacterized YcaO from Escherichia coli (Ec-YcaO). Ec-YcaO harbors an unprecedented fold and ATP-binding motif. This motif is conserved among TOMM YcaOs and is required for cyclodehydration. Furthermore, we demonstrate that the C protein regulates substrate binding and catalysis and that the proline-rich C terminus of the D protein is involved in C protein recognition and catalysis. This study identifies the YcaO active site and paves the way for the characterization of the numerous YcaO domains not associated with TOMM biosynthesis.

PubMed: 25129028
DOI: 10.1038/nchembio.1608

実験手法

X-RAY DIFFRACTION (2.64 Å)