5M9X

Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to glycosylated resveratrol

Summary for 5M9X

• Entry DOI: 10.2210/pdb5m9x/pdb
• Related: 5C8B
• Descriptor: Sucrose phosphorylase, (2~{R},3~{S},4~{S},5~{R},6~{R})-2-(hydroxymethyl)-6-[3-[(~{E})-2-(4-hydroxyphenyl)ethenyl]-5-oxidanyl-phenoxy]oxane-3,4 ,5-triol (3 entities in total)
• Functional Keywords: sucrose phosphorylase, resveratrol, enzyme design, transferase
• Biological source: Bifidobacterium adolescentis
• Total number of polymer chains: 1
• Total formula weight: 56661.11

Authors

Grimm, C.,Kraus, M. (deposition date: 2016-11-02, release date: 2017-12-20, Last modification date: 2024-05-08)

Primary citation

Kraus, M.,Grimm, C.,Seibel, J.
Switching enzyme specificity from phosphate to resveratrol glucosylation.
Chem. Commun. (Camb.), 53:12181-12184, 2017

PubMed Abstract: Here we present a point mutation-triggered domain shift which switches the acceptor preference of a sucrose phosphorylase from phosphate to a variety of large polyphenolic compounds including resveratrol and quercetin, enabling their efficient glucosylation. The variant possesses a high affinity for aromatic substrates due to newly introduced π-π- and hydrophobic interactions in the altered active site. The domain shift brings about a substantially enlarged and multifunctional active site for polyphenol glucosylation and rare disaccharide production. The crystal structure of the variant with its product resveratrol-3-α-d-glucoside allows the prediction of the substrate scope and regioselectivity of the aromatic compounds' glucosylation sites.

PubMed: 29057405
DOI: 10.1039/c7cc05993k

Experimental method

X-RAY DIFFRACTION (2.349 Å)