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6A8H

Crystal structure of endo-arabinanase ABN-TS D27A mutant in complex with arabinotriose

6A8H の概要
エントリーDOI10.2210/pdb6a8h/pdb
分子名称endo-alpha-(1->5)-L-arabinanase, alpha-L-arabinofuranose-(1-5)-alpha-L-arabinofuranose-(1-5)-alpha-L-arabinofuranose, CALCIUM ION, ... (5 entities in total)
機能のキーワードarabinanase, thermostable enzyme, glycoside hydrolase, gh43, hydrolase
由来する生物種Geobacillus thermodenitrificans
タンパク質・核酸の鎖数1
化学式量合計37407.82
構造登録者
Yamaguchi, A.,Tada, T. (登録日: 2018-07-09, 公開日: 2018-12-19, 最終更新日: 2024-11-06)
主引用文献Yamaguchi, A.,Sogabe, Y.,Fukuoka, S.,Sakai, T.,Tada, T.
Structures of endo-1,5-alpha-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides.
Acta Crystallogr F Struct Biol Commun, 74:774-780, 2018
Cited by
PubMed Abstract: The thermostable endo-1,5-α-L-arabinanase from Bacillus thermodenitrificans TS-3 (ABN-TS) hydrolyzes the α-1,5-L-arabinofuranoside linkages of arabinan. In this study, the crystal structures of inactive ABN-TS mutants, D27A and D147N, were determined in complex with arabino-oligosaccharides. The crystal structures revealed that ABN-TS has at least six subsites in the deep V-shaped cleft formed across one face of the propeller structure. The structural features indicate that substrate recognition is profoundly influenced by the remote subsites as well as by the subsites surrounding the active center. The `open' structure of the substrate-binding cleft of the endo-acting ABN-TS is suitable for the random binding of several sugar units in polymeric substrates.
PubMed: 30511671
DOI: 10.1107/S2053230X18015947
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.65 Å)
構造検証レポート
Validation report summary of 6a8h
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2025-06-18に公開中

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