3QL0

Crystal structure of N23PP/S148A mutant of E. coli dihydrofolate reductase

3QL0 の概要

• エントリーDOI: 10.2210/pdb3ql0/pdb
• 関連するPDBエントリー: 3QL3
• 分子名称: Dihydrofolate reductase, FOLIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: rossmann fold, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19337.24

構造登録者

Bhabha, G.,Ekiert, D.C.,Wright, P.E.,Wilson, I.A. (登録日: 2011-02-02, 公開日: 2011-04-20, 最終更新日: 2024-02-21)

主引用文献

Bhabha, G.,Lee, J.,Ekiert, D.C.,Gam, J.,Wilson, I.A.,Dyson, H.J.,Benkovic, S.J.,Wright, P.E.
A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis.
Science, 332:234-238, 2011

PubMed Abstract: Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we have found a link between conformational fluctuations on the millisecond time scale and the chemical step of an enzymatic reaction, with broad implications for our understanding of enzyme mechanisms and for design of novel protein catalysts.

PubMed: 21474759
DOI: 10.1126/science.1198542

実験手法

X-RAY DIFFRACTION (1.6 Å)