7L1Y
Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortium-xylobiose complex
Summary for 7L1Y
| Entry DOI | 10.2210/pdb7l1y/pdb |
| Related PRD ID | PRD_900116 |
| Descriptor | Exo-B-1,4-beta-xylanase, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | glycoside hydrolase family 11, gh11, exo-b-1, 4-xylobiosidase, hydrolase |
| Biological source | unidentified |
| Total number of polymer chains | 1 |
| Total formula weight | 28149.94 |
| Authors | Kadowaki, M.A.S.,Polikarpov, I.,Briganti, L.,Evangelista, D.E. (deposition date: 2020-12-15, release date: 2021-07-28, Last modification date: 2023-10-18) |
| Primary citation | Kadowaki, M.A.S.,Briganti, L.,Evangelista, D.E.,Echevarria-Poza, A.,Tryfona, T.,Pellegrini, V.O.A.,Nakayama, D.G.,Dupree, P.,Polikarpov, I. Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium. Biotechnol.Bioeng., 118:4052-4064, 2021 Cited by PubMed Abstract: The heteropolysaccharide xylan is a valuable source of sustainable chemicals and materials from renewable biomass sources. A complete hydrolysis of this major hemicellulose component requires a diverse set of enzymes including endo-β-1,4-xylanases, β-xylosidases, acetylxylan esterases, α-l-arabinofuranosidases, and α-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-β-1,4- and β-1,3-xylanases. However, a recent analysis of a metatranscriptome library from a microbial lignocellulose community revealed GH11 enzymes capable of releasing solely xylobiose from xylan. Although initial biochemical studies clearly indicated their xylobiohydrolase mode of action, the structural features that drive this new activity still remained unclear. It was also not clear whether the enzymes acted on the reducing or nonreducing end of the substrate. Here, we solved the crystal structure of MetXyn11 in the apo and xylobiose-bound forms. The structure of MetXyn11 revealed the molecular features that explain the observed pattern on xylooligosaccharides released by this nonreducing end xylobiohydrolase. PubMed: 34232504DOI: 10.1002/bit.27880 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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