4EL8
The unliganded structure of C.bescii CelA GH48 module
4EL8 の概要
エントリーDOI | 10.2210/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 | |
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: 24357319DOI: 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) |
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