4dod | pdb_00004dod

The structure of Cbescii CelA GH9 module

spinqualitylabelsall models 4dod, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4dod is a 1 chain structure with sequence from "anaerocellum_thermophilum"_svetlichnyi_va_et_al._1990 "anaerocellum thermophilum" svetlichnyi va et al. 1990. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, DIO, EDO, GOL, SO4 Related: 4doe Gene: celA ("Anaerocellum thermophilum" Svetlichnyi VA et al. 1990) Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA.,Brunecky R, Alahuhta M, Xu Q, Donohoe BS, Crowley MF, Kataeva IA, Yang SJ, Resch MG, Adams MW, Lunin VV, Himmel ME, Bomble YJ Science. 2013 Dec 20;342(6165):1513-6. doi: 10.1126/science.1244273. PMID:24357319 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glucanase

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