6GH7

WILDTYPE CORE-STREPTAVIDIN WITH a conjugated BIOTINYLATED PYRROLIDINE

Summary for 6GH7

• Entry DOI: 10.2210/pdb6gh7/pdb
• Descriptor: Streptavidin, 5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]-~{N}-[(3~{R})-pyrrolidin-3-yl]pentanamide (3 entities in total)
• Functional Keywords: biotin-binding protein, organocatalysis, supramolecular chemistry, secondary amine, artificial enzyme
• Biological source: Streptomyces avidinii
• Total number of polymer chains: 4
• Total formula weight: 54899.85

Authors

Nodling, A.R.,Tsai, Y.H.,Luk, L.Y.P.,Rizkallah, P.,Jin, Y. (deposition date: 2018-05-04, release date: 2018-10-10, Last modification date: 2024-01-17)

Primary citation

Nodling, A.R.,Swiderek, K.,Castillo, R.,Hall, J.W.,Angelastro, A.,Morrill, L.C.,Jin, Y.,Tsai, Y.H.,Moliner, V.,Luk, L.Y.P.
Reactivity and Selectivity of Iminium Organocatalysis Improved by a Protein Host.
Angew.Chem.Int.Ed.Engl., 57:12478-12482, 2018

PubMed Abstract: There has been growing interest in performing organocatalysis within a supramolecular system as a means of controlling reaction reactivity and stereoselectivity. Here, a protein is used as a host for iminium catalysis. A pyrrolidine moiety is covalently linked to biotin and introduced to the protein host streptavidin for organocatalytic activity. Whereas in traditional systems stereoselectivity is largely controlled by the substituents added to the organocatalyst, enantiomeric enrichment by the reported supramolecular system is completely controlled by the host. Also, the yield of the model reaction increases over 10-fold when streptavidin is included. A 1.1 Å crystal structure of the protein-catalyst complex and molecular simulations of a key intermediate reveal the chiral scaffold surrounding the organocatalytic reaction site. This work illustrates that proteins can be an excellent supramolecular host for driving stereoselective secondary amine organocatalysis.

PubMed: 30027571
DOI: 10.1002/anie.201806850

Experimental method

X-RAY DIFFRACTION (1.08 Å)