5MAN
Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose
Summary for 5MAN
| Entry DOI | 10.2210/pdb5man/pdb |
| Related PRD ID | PRD_900052 |
| Descriptor | Sucrose phosphorylase, alpha-D-glucopyranose-(1-3)-alpha-D-glucopyranose (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 | 56613.02 |
| Authors | |
| Primary citation | Kraus, M.,Grimm, C.,Seibel, J. Switching enzyme specificity from phosphate to resveratrol glucosylation. Chem. Commun. (Camb.), 53:12181-12184, 2017 Cited by 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: 29057405DOI: 10.1039/c7cc05993k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
Download full validation report
