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4EL8

The unliganded structure of C.bescii CelA GH48 module

4EL8 の概要
エントリーDOI10.2210/pdb4el8/pdb
分子名称Glycoside hydrolase family 48, CALCIUM ION, SULFATE ION, ... (5 entities in total)
機能のキーワード(a/a)6 barre, cela, gh48, glycoside hydrolase, hydrolase
由来する生物種Caldicellulosiruptor bescii
タンパク質・核酸の鎖数1
化学式量合計72436.48
構造登録者
Alahuhta, P.M.,Lunin, V.V. (登録日: 2012-04-10, 公開日: 2013-03-20, 最終更新日: 2023-09-13)
主引用文献Brunecky, R.,Alahuhta, M.,Xu, Q.,Donohoe, B.S.,Crowley, M.F.,Kataeva, I.A.,Yang, S.J.,Resch, M.G.,Adams, M.W.,Lunin, V.V.,Himmel, M.E.,Bomble, Y.J.
Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA.
Science, 342:1513-1516, 2013
Cited by
PubMed Abstract: Most fungi and bacteria degrade plant cell walls by secreting free, complementary enzymes that hydrolyze cellulose; however, some bacteria use large enzymatic assemblies called cellulosomes, which recruit complementary enzymes to protein scaffolds. The thermophilic bacterium Caldicellulosiruptor bescii uses an intermediate strategy, secreting many free cellulases that contain multiple catalytic domains. One of these, CelA, comprises a glycoside hydrolase family 9 and a family 48 catalytic domain, as well as three type III cellulose-binding modules. In the saccharification of a common cellulose standard, Avicel, CelA outperforms mixtures of commercially relevant exo- and endoglucanases. From transmission electron microscopy studies of cellulose after incubation with CelA, we report morphological features that suggest that CelA not only exploits the common surface ablation mechanism driven by general cellulase processivity, but also excavates extensive cavities into the surface of the substrate. These results suggest that nature's repertoire of cellulose digestion paradigms remain only partially discovered and understood.
PubMed: 24357319
DOI: 10.1126/science.1244273
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.45 Å)
構造検証レポート
Validation report summary of 4el8
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2025-02-05に公開中

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