4GJV

Streptavidin-S112H

Summary for 4GJV

• Entry DOI: 10.2210/pdb4gjv/pdb
• Descriptor: 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+), CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: artificial metalloenyzme, artificial transfer hydrogenase, beta barrel, tetramer, biotin, iridium pentamethylcyclopentadienyl, biotin-binding protein
• Biological source: Streptomyces avidinii
• Cellular location: Secreted: P22629
• Total number of polymer chains: 1
• Total formula weight: 17465.63

Authors

Heinisch, T.,Schirmer, T. (deposition date: 2012-08-10, release date: 2013-02-13, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)