3WC4
Crystal structure of UDP-glucose: anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea
Summary for 3WC4
| Entry DOI | 10.2210/pdb3wc4/pdb |
| Descriptor | UDP-glucose:anthocyanidin 3-O-glucosyltransferase, GLYCEROL, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | gt-b fold, glucosyltransferase, udp-glucose/anthocyanidin binding, glucosylation, transferase |
| Biological source | Clitoria ternatea (Butterfly pea) |
| Total number of polymer chains | 1 |
| Total formula weight | 49020.48 |
| Authors | Hiromoto, T.,Honjo, E.,Tamada, T.,Kuroki, R. (deposition date: 2013-05-24, release date: 2013-10-30, Last modification date: 2023-11-08) |
| Primary citation | Hiromoto, T.,Honjo, E.,Tamada, T.,Noda, N.,Kazuma, K.,Suzuki, M.,Kuroki, R. Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea J.SYNCHROTRON RADIAT., 20:894-898, 2013 Cited by PubMed Abstract: Flowers of the butterfly pea (Clitoria ternatea) accumulate a group of polyacylated anthocyanins, named ternatins, in their petals. The first step in ternatin biosynthesis is the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin, a reaction catalyzed in C. ternatea by UDP-glucose:anthocyanidin 3-O-glucosyltransferase (Ct3GT-A; AB185904). To elucidate the structure-function relationship of Ct3GT-A, recombinant Ct3GT-A was expressed in Escherichia coli and its tertiary structure was determined to 1.85 Å resolution by using X-ray crystallography. The structure of Ct3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like β/α/β domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrates. By comparing the structure of Ct3GT-A with that of the flavonoid glycosyltransferase VvGT1 from red grape (Vitis vinifera) in complex with UDP-2-deoxy-2-fluoro glucose and kaempferol, locations of the catalytic His-Asp dyad and the residues involved in recognizing UDP-2-deoxy-2-fluoro glucose were essentially identical in Ct3GT-A, but certain residues of VvGT1 involved in binding kaempferol were found to be substituted in Ct3GT-A. These findings are important for understanding the differentiation of acceptor-substrate recognition in these two enzymes. PubMed: 24121335DOI: 10.1107/S0909049513020712 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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