8Y2H

GK tetramer of AtP5CS1 filament with adjacent hooks, reaction state

8Y2H の概要

• エントリーDOI: 10.2210/pdb8y2h/pdb
• 関連するPDBエントリー: 8J0F
• EMDBエントリー: 35901 38855
• 分子名称: Delta-1-pyrroline-5-carboxylate synthase A, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: l-proline biosynthesis, filamentous enzyme, transferase, plant protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 633973.41

構造登録者

Zhang, T.,Guo, C.J.,Liu, J.L. (登録日: 2024-01-26, 公開日: 2024-06-05, 最終更新日: 2024-07-10)

主引用文献

Guo, C.J.,Zhang, T.,Leng, Q.,Zhou, X.,Zhong, J.,Liu, J.L.
Dynamic Arabidopsis P5CS filament facilitates substrate channelling.
Nat.Plants, 10:880-889, 2024

PubMed Abstract: In plants, the rapid accumulation of proline is a common response to combat abiotic stress. Delta-1-pyrroline-5-carboxylate synthase (P5CS) is a rate-limiting enzyme in proline synthesis, catalysing the initial two-step conversion from glutamate to proline. Here we determine the first structure of plant P5CS. Our results show that Arabidopsis thaliana P5CS1 (AtP5CS1) and P5CS2 (AtP5CS2) can form enzymatic filaments in a substrate-sensitive manner. The destruction of AtP5CS filaments by mutagenesis leads to a significant reduction in enzymatic activity. Furthermore, separate activity tests on two domains reveal that filament-based substrate channelling is essential for maintaining the high catalytic efficiency of AtP5CS. Our study demonstrates the unique mechanism for the efficient catalysis of AtP5CS, shedding light on the intricate mechanisms underlying plant proline metabolism and stress response.

PubMed: 38740943
DOI: 10.1038/s41477-024-01697-w

実験手法

ELECTRON MICROSCOPY (3.3 Å)