4GJS

Streptavidin-K121H

4GJS の概要

• エントリーDOI: 10.2210/pdb4gjs/pdb
• 分子名称: Streptavidin, trichloro{(1,2,3,4,5-eta)-1,2,3,4-tetramethyl-5-[2-({5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanoyl}amino)ethyl]cyclopentadienyl}rhodium(1+), Rhodium, ... (4 entities in total)
• 機能のキーワード: artificial metalloenyzme, artificial transfer hydrogenase, beta barrel, tetramer, biotin, iridium pentamethylcyclopentadienyl, 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: 2
• 化学式量合計: 34563.43

構造登録者

Heinisch, T.,Schirmer, T. (登録日: 2012-08-10, 公開日: 2013-02-13, 最終更新日: 2024-02-28)

主引用文献

Zimbron, J.M.,Heinisch, T.,Schmid, M.,Hamels, D.,Nogueira, E.S.,Schirmer, T.,Ward, T.R.
A dual anchoring strategy for the localization and activation of artificial metalloenzymes based on the biotin-streptavidin technology.
J.Am.Chem.Soc., 135:5384-5388, 2013

PubMed Abstract: Artificial metalloenzymes result from anchoring an active catalyst within a protein environment. Toward this goal, various localization strategies have been pursued: covalent, supramolecular, or dative anchoring. Herein we show that introduction of a suitably positioned histidine residue contributes to firmly anchor, via a dative bond, a biotinylated rhodium piano stool complex within streptavidin. The in silico design of the artificial metalloenzyme was confirmed by X-ray crystallography. The resulting artificial metalloenzyme displays significantly improved catalytic performance, both in terms of activity and selectivity in the transfer hydrogenation of imines. Depending on the position of the histidine residue, both enantiomers of the salsolidine product can be obtained.

PubMed: 23496309
DOI: 10.1021/ja309974s

実験手法

X-RAY DIFFRACTION (1.85 Å)