7l1w

Unlocking the structural features for the exo-xylobiosidase activity of an unusual GH11 member identified in a compost-derived consortium

spinqualitylabelsall models 7l1w, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7l1w is a 1 chain structure with sequence from Unidentified. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.71Å Ligands: MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2H4TGG5_9BACT Publication Abstract from PubMed 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-beta-1,4-xylanases, beta-xylosidases, acetylxylan esterases, alpha-l-arabinofuranosidases, and alpha-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-beta-1,4- and beta-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. Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium.,Kadowaki MAS, Briganti L, Evangelista DE, Echevarria-Poza A, Tryfona T, Pellegrini VOA, Nakayama DG, Dupree P, Polikarpov I Biotechnol Bioeng. 2021 Jul 7. doi: 10.1002/bit.27880. PMID:34232504 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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