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4WHM

Crystal structure of UDP-glucose: anthocyanidin 3-O-glucosyltransferase in complex with UDP

4WHM の概要
エントリーDOI10.2210/pdb4whm/pdb
関連するPDBエントリー3WC4 4REL 4REM 4REN
分子名称UDP-glucose:anthocyanidin 3-O-glucosyltransferase, URIDINE-5'-DIPHOSPHATE, GLYCEROL, ... (5 entities in total)
機能のキーワードct3gt-a, ugt78k6, gt-b fold, complexed with udp, 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49424.64
構造登録者
Hiromoto, T.,Honjo, E.,Tamada, T.,Kuroki, R. (登録日: 2014-09-23, 公開日: 2015-01-21, 最終更新日: 2023-11-08)
主引用文献Hiromoto, T.,Honjo, E.,Noda, N.,Tamada, T.,Kazuma, K.,Suzuki, M.,Blaber, M.,Kuroki, R.
Structural basis for acceptor-substrate recognition of UDP-glucose: anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea
Protein Sci., 24:395-407, 2015
Cited by
PubMed Abstract: UDP-glucose: anthocyanidin 3-O-glucosyltransferase (UGT78K6) from Clitoria ternatea catalyzes the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin. After the acylation of the 3-O-glucosyl residue, the 3'- and 5'-hydroxyl groups of the product are further glucosylated by a glucosyltransferase in the biosynthesis of ternatins, which are anthocyanin pigments. To understand the acceptor-recognition scheme of UGT78K6, the crystal structure of UGT78K6 and its complex forms with anthocyanidin delphinidin and petunidin, and flavonol kaempferol were determined to resolutions of 1.85 Å, 2.55 Å, 2.70 Å, and 1.75 Å, respectively. The enzyme recognition of unstable anthocyanidin aglycones was initially observed in this structural determination. The anthocyanidin- and flavonol-acceptor binding details are almost identical in each complex structure, although the glucosylation activities against each acceptor were significantly different. The 3-hydroxyl groups of the acceptor substrates were located at hydrogen-bonding distances to the Nε2 atom of the His17 catalytic residue, supporting a role for glucosyl transfer to the 3-hydroxyl groups of anthocyanidins and flavonols. However, the molecular orientations of these three acceptors are different from those of the known flavonoid glycosyltransferases, VvGT1 and UGT78G1. The acceptor substrates in UGT78K6 are reversely bound to its binding site by a 180° rotation about the O1-O3 axis of the flavonoid backbones observed in VvGT1 and UGT78G1; consequently, the 5- and 7-hydroxyl groups are protected from glucosylation. These substrate recognition schemes are useful to understand the unique reaction mechanism of UGT78K6 for the ternatin biosynthesis, and suggest the potential for controlled synthesis of natural pigments.
PubMed: 25556637
DOI: 10.1002/pro.2630
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.851 Å)
構造検証レポート
Validation report summary of 4whm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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