3SK0

structure of Rhodococcus rhodochrous haloalkane dehalogenase DhaA mutant DhaA12

3SK0 の概要

• エントリーDOI: 10.2210/pdb3sk0/pdb
• 関連するPDBエントリー: 1BN6 1CQW
• 分子名称: Haloalkane dehalogenase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: catalytic pentad, alpha/beta-hydrolase fold, hydrolase, halide binding, hydrolytic dehalogenation
• 由来する生物種: Rhodococcus rhodochrous
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35432.50

構造登録者

Lahoda, M.,Stsiapanava, A.,Mesters, J.,Koudelakova, T.,Damborsky, J.,Kuta-Smatanova, I. (登録日: 2011-06-22, 公開日: 2012-06-27, 最終更新日: 2023-09-13)

主引用文献

Sykora, J.,Brezovsky, J.,Koudelakova, T.,Lahoda, M.,Fortova, A.,Chernovets, T.,Chaloupkova, R.,Stepankova, V.,Prokop, Z.,Smatanova, I.K.,Hof, M.,Damborsky, J.
Dynamics and hydration explain failed functional transformation in dehalogenase design.
Nat.Chem.Biol., 10:428-430, 2014

PubMed Abstract: We emphasize the importance of dynamics and hydration for enzymatic catalysis and protein design by transplanting the active site from a haloalkane dehalogenase with high enantioselectivity to nonselective dehalogenase. Protein crystallography confirms that the active site geometry of the redesigned dehalogenase matches that of the target, but its enantioselectivity remains low. Time-dependent fluorescence shifts and computer simulations revealed that dynamics and hydration at the tunnel mouth differ substantially between the redesigned and target dehalogenase.

PubMed: 24727901
DOI: 10.1038/nchembio.1502

実験手法

X-RAY DIFFRACTION (1.78 Å)