3WC4

Crystal structure of UDP-glucose: anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea

3WC4 の概要

• エントリーDOI: 10.2210/pdb3wc4/pdb
• 分子名称: UDP-glucose:anthocyanidin 3-O-glucosyltransferase, GLYCEROL, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: gt-b fold, glucosyltransferase, udp-glucose/anthocyanidin binding, glucosylation, transferase
• 由来する生物種: Clitoria ternatea (Butterfly pea)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49020.48

構造登録者

Hiromoto, T.,Honjo, E.,Tamada, T.,Kuroki, R. (登録日: 2013-05-24, 公開日: 2013-10-30, 最終更新日: 2023-11-08)

主引用文献

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

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: 24121335
DOI: 10.1107/S0909049513020712

実験手法

X-RAY DIFFRACTION (1.85 Å)