5C2X

Crystal structure of deoxyribose-phosphate aldolase from Colwellia psychrerythraea (tetragonal form)

5C2X の概要

• エントリーDOI: 10.2210/pdb5c2x/pdb
• 分子名称: Deoxyribose-phosphate aldolase, UNKNOWN LIGAND, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: dera, tim barrel, psychrophilic, lyase
• 由来する生物種: Colwellia psychrerythraea
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57120.89

構造登録者

Dick, M.,Weiergraeber, O.H.,Pietruszka, J. (登録日: 2015-06-16, 公開日: 2016-02-03, 最終更新日: 2024-11-13)

主引用文献

Dick, M.,Weiergraber, O.H.,Classen, T.,Bisterfeld, C.,Bramski, J.,Gohlke, H.,Pietruszka, J.
Trading off stability against activity in extremophilic aldolases.
Sci Rep, 6:17908-17908, 2016

PubMed Abstract: Understanding enzyme stability and activity in extremophilic organisms is of great biotechnological interest, but many questions are still unsolved. Using 2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model enzyme, we have evaluated structural and functional characteristics of different orthologs from psychrophilic, mesophilic and hyperthermophilic organisms. We present the first crystal structures of psychrophilic DERAs, revealing a dimeric organization resembling their mesophilic but not their thermophilic counterparts. Conversion into monomeric proteins showed that the native dimer interface contributes to stability only in the hyperthermophilic enzymes. Nevertheless, introduction of a disulfide bridge in the interface of a psychrophilic DERA did confer increased thermostability, suggesting a strategy for rational design of more durable enzyme variants. Constraint network analysis revealed particularly sparse interactions between the substrate pocket and its surrounding α-helices in psychrophilic DERAs, which indicates that a more flexible active center underlies their high turnover numbers.

PubMed: 26783049
DOI: 10.1038/srep17908

実験手法

X-RAY DIFFRACTION (2.11 Å)