5LU6

Heptose isomerase mutant - H64Q

5LU6 の概要

• エントリーDOI: 10.2210/pdb5lu6/pdb
• 分子名称: Phosphoheptose isomerase, D-ALTRO-HEPT-2-ULOSE 7-PHOSPHATE, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: cooperativity, enzyme kinetics, hydrogen bonds, molecular modelling, quantum mechanics, isomerase
• 由来する生物種: Burkholderia pseudomallei
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 84683.86

構造登録者

Vivoli, M.,Harmer, N.J.,Pang, J. (登録日: 2016-09-08, 公開日: 2017-12-06, 最終更新日: 2024-05-08)

主引用文献

Vivoli, M.,Pang, J.,Harmer, N.J.
A half-site multimeric enzyme achieves its cooperativity without conformational changes.
Sci Rep, 7:16529-16529, 2017

PubMed Abstract: Cooperativity is a feature many multimeric proteins use to control activity. Here we show that the bacterial heptose isomerase GmhA displays homotropic positive and negative cooperativity among its four protomers. Most similar proteins achieve this through conformational changes: GmhA instead employs a delicate network of hydrogen bonds, and couples pairs of active sites controlled by a unique water channel. This network apparently raises the Lewis acidity of the catalytic zinc, thus increasing the activity at one active site at the cost of preventing substrate from adopting a reactive conformation at the paired negatively cooperative site - a "half-site" behavior. Our study establishes the principle that multimeric enzymes can exploit this cooperativity without conformational changes to maximize their catalytic power and control. More broadly, this subtlety by which enzymes regulate functions could be used to explore new inhibitor design strategies.

PubMed: 29184087
DOI: 10.1038/s41598-017-16421-2

実験手法

X-RAY DIFFRACTION (1.67 Å)