3WMR

Crystal structure of VinJ

3WMR の概要

• エントリーDOI: 10.2210/pdb3wmr/pdb
• 分子名称: Proline iminopeptidase, GLYCEROL, 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase fold, hydrolase
• 由来する生物種: Streptomyces halstedii
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 107710.79

構造登録者

Shinohara, Y.,Miyanaga, A.,Kudo, F.,Eguchi, T. (登録日: 2013-11-22, 公開日: 2014-02-05, 最終更新日: 2023-11-08)

主引用文献

Shinohara, Y.,Miyanaga, A.,Kudo, F.,Eguchi, T.
The crystal structure of the amidohydrolase VinJ shows a unique hydrophobic tunnel for its interaction with polyketide substrates
Febs Lett., 588:995-1000, 2014

PubMed Abstract: VinJ is an amidohydrolase belonging to the serine peptidase family that catalyzes the hydrolysis of the terminal aminoacyl moiety of a polyketide intermediate during the biosynthesis of vicenistatin. Herein, we report the crystal structure of VinJ. VinJ possesses a unique hydrophobic tunnel for the recognition of the polyketide chain moiety of its substrate in the cap domain. Taken together with the results of phylogenetic analysis, our results suggest that VinJ represents a new amidohydrolase family that is different from the known α/β hydrolase type serine peptidases.

PubMed: 24530530
DOI: 10.1016/j.febslet.2014.01.060

実験手法

X-RAY DIFFRACTION (1.95 Å)