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6IK7

Crystal structure of tomato beta-galactosidase (TBG) 4 in complex with beta-1,3-galactobiose

6IK7 の概要
エントリーDOI10.2210/pdb6ik7/pdb
分子名称Beta-galactosidase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-galactopyranose-(1-3)-beta-D-galactopyranose, ... (5 entities in total)
機能のキーワードglycoside hydrolase, plant, plant cell wall related enzyme, fruit ripening, hydrolase
由来する生物種Solanum lycopersicum (Tomato)
タンパク質・核酸の鎖数2
化学式量合計161429.64
構造登録者
Matsuyama, K.,Nakae, S.,Igarashi, K.,Tada, T.,Ishimaru, M. (登録日: 2018-10-15, 公開日: 2018-11-28, 最終更新日: 2024-11-13)
主引用文献Matsuyama, K.,Kondo, T.,Igarashi, K.,Sakamoto, T.,Ishimaru, M.
Substrate-recognition mechanism of tomato beta-galactosidase 4 using X-ray crystallography and docking simulation.
Planta, 252:72-72, 2020
Cited by
PubMed Abstract: TBG4 recognize multiple linkage types substrates due to having a spatially wide subsite + 1. This feature allows the degradation of AGI, AGII, and AGP leading to the fruit ripening. β-galactosidase (EC 3. 2. 1. 23) catalyzes the hydrolysis of β-galactan and release of D-galactose. Tomato has at least 17 β-galactosidases (TBGs), of which, TBG 4 is responsible for fruit ripening. TBG4 hydrolyzes not only β-1,4-bound galactans, but also β-1,3- and β-1,6-galactans. In this study, we compared each enzyme-substrate complex using X-ray crystallography, ensemble refinement, and docking simulation to understand the broad substrate-specificity of TBG4. In subsite - 1, most interactions were conserved across each linkage type of galactobioses; however, some differences were seen in subsite + 1, owing to the huge volume of catalytic pocket. In addition to this, docking simulation indicated TBG4 to possibly have more positive subsites to recognize and hydrolyze longer galactans. Taken together, our results indicated that during tomato fruit ripening, TBG4 plays an important role by degrading arabinogalactan I (AGI), arabinogalactan II (AGII), and the carbohydrate moiety of arabinogalactan protein (AGP).
PubMed: 33011862
DOI: 10.1007/s00425-020-03481-4
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.1 Å)
構造検証レポート
Validation report summary of 6ik7
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2026-04-15に公開中

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