5MLP

Structure of CDPS from Rickettsiella grylli

5MLP の概要

• エントリーDOI: 10.2210/pdb5mlp/pdb
• 関連するPDBエントリー: 4Q24
• 分子名称: Uncharacterized protein (2 entities in total)
• 機能のキーワード: cyclodipeptide synthase, ligase
• 由来する生物種: Rickettsiella grylli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31486.75

構造登録者

Bourgeois, G.,Seguin, J.,Moutiez, M.,Babin, M.,Belin, P.,Mechulam, Y.,Gondry, M.,Schmitt, E. (登録日: 2016-12-07, 公開日: 2018-05-02, 最終更新日: 2024-10-23)

主引用文献

Bourgeois, G.,Seguin, J.,Babin, M.,Belin, P.,Moutiez, M.,Mechulam, Y.,Gondry, M.,Schmitt, E.
Structural basis for partition of the cyclodipeptide synthases into two subfamilies.
J.Struct.Biol., 203:17-26, 2018

PubMed Abstract: Cyclodipeptide synthases (CDPSs) use two aminoacyl-tRNAs to catalyze the formation of two peptide bonds leading to cyclodipeptides that can be further used for the synthesis of diketopiperazines. It was shown that CDPSs fall into two subfamilies, NYH and XYP, characterized by the presence of specific sequence signatures. However, current understanding of CDPSs only comes from studies of enzymes from the NYH subfamily. The present study reveals the crystal structures of three CDPSs from the XYP subfamily. Comparison of the XYP and NYH enzymes shows that the two subfamilies mainly differ in the first half of their Rossmann fold. This gives a structural basis for the partition of CDPSs into two subfamilies. Despite these differences, the catalytic residues adopt similar positioning regardless of the subfamily suggesting that the XYP and NYH motifs correspond to two structural solutions to facilitate the reactivity of the catalytic serine residue.

PubMed: 29505829
DOI: 10.1016/j.jsb.2018.03.001

実験手法

X-RAY DIFFRACTION (1.99 Å)