6NPS
Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus
Summary for 6NPS
| Entry DOI | 10.2210/pdb6nps/pdb |
| Descriptor | AxyAgu115A, CHLORIDE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | gylcosyl hydrolase family 115, gh115, hemicellulase, arabinoglucuronoxylan, sugar binding protein, glucuronidase, glucuronic acid, hydrolase |
| Biological source | Amphibacillus xylanus NBRC 15112 |
| Total number of polymer chains | 2 |
| Total formula weight | 222041.25 |
| Authors | Stogios, P.J.,Skarina, T.,Di Leo, R.,Yan, R.,Master, E.,Savchenko, A. (deposition date: 2019-01-18, release date: 2020-07-15, Last modification date: 2023-10-11) |
| Primary citation | Yan, R.,Wang, W.,Vuong, T.V.,Xiu, Y.,Skarina, T.,Di Leo, R.,Gatenholm, P.,Toriz, G.,Tenkanen, M.,Stogios, P.J.,Master, E.R. Structural characterization of the family GH115 alpha-glucuronidase from Amphibacillus xylanus yields insight into its coordinated action with alpha-arabinofuranosidases. N Biotechnol, 2021 Cited by PubMed Abstract: The coordinated action of carbohydrate-active enzymes has mainly been evaluated for the purpose of complete saccharification of plant biomass (lignocellulose) to sugars. By contrast, the coordinated action of accessory hemicellulases on xylan debranching and recovery is less well characterized. Here, the activity of two family GH115 α-glucuronidases (SdeAgu115A from Saccharophagus degradans, and AxyAgu115A from Amphibacillus xylanus) on spruce arabinoglucuronoxylan (AGX) was evaluated in combination with an α-arabinofuranosidase from families GH51 (AniAbf51A, aka E-AFASE from Aspergillus niger) and GH62 (SthAbf62A from Streptomyces thermoviolaceus). The α-arabinofuranosidases boosted (methyl)-glucuronic acid release by SdeAgu115A by approximately 50 % and 30 %, respectively. The impact of the α-arabinofuranosidases on AxyAgu115A activity was comparatively low, motivating its structural characterization. The crystal structure of AxyAgu115A revealed increased length and flexibility of the active site loop compared to SdeAgu115A. This structural difference could explain the ability of AxyAgu115A to accommodate more highly substituted arabinoglucuronoxylan, and inform enzyme selections for improved AGX recovery and use. PubMed: 33486119DOI: 10.1016/j.nbt.2021.01.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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