6ESS

Artificial imine reductase mutant S112A-N118P-K121A-S122M

6ESS の概要

• エントリーDOI: 10.2210/pdb6ess/pdb
• 分子名称: Streptavidin, {N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide}(chloro)[(1,2,3,4,5-eta)-1,2,3,4,5-pentamethylcyclopentadienyl]iridium(III), IRIDIUM ION, ... (4 entities in total)
• 機能のキーワード: streptavidin, beta-barrel, biotin-binding protein
• 由来する生物種: Streptomyces avidinii
• 細胞内の位置: Secreted: P22629
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17907.18

構造登録者

Hestericova, M.,Heinisch, T.,Alonso-Cotchico, L.,Marechal, J.-D.,Vidossich, P.,Ward, T.R. (登録日: 2017-10-24, 公開日: 2018-01-03, 最終更新日: 2024-05-08)

主引用文献

Hestericova, M.,Heinisch, T.,Alonso-Cotchico, L.,Marechal, J.D.,Vidossich, P.,Ward, T.R.
Directed Evolution of an Artificial Imine Reductase.
Angew. Chem. Int. Ed. Engl., 57:1863-1868, 2018

PubMed Abstract: Artificial metalloenzymes, resulting from incorporation of a metal cofactor within a host protein, have received increasing attention in the last decade. The directed evolution is presented of an artificial transfer hydrogenase (ATHase) based on the biotin-streptavidin technology using a straightforward procedure allowing screening in cell-free extracts. Two streptavidin isoforms were yielded with improved catalytic activity and selectivity for the reduction of cyclic imines. The evolved ATHases were stable under biphasic catalytic conditions. The X-ray structure analysis reveals that introducing bulky residues within the active site results in flexibility changes of the cofactor, thus increasing exposure of the metal to the protein surface and leading to a reversal of enantioselectivity. This hypothesis was confirmed by a multiscale approach based mostly on molecular dynamics and protein-ligand dockings.

PubMed: 29265726
DOI: 10.1002/anie.201711016

実験手法

X-RAY DIFFRACTION (1.91 Å)