5cg0

Crystal structure of Spodoptera frugiperda Beta-glycosidase

spinqualitylabelsall models 5cg0, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cg0 is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The active site residues in GH1 beta-glycosidases are compartmentalized into 3 functional regions, involved in catalysis or binding of glycone and aglycone motifs from substrate. However, it still remains unclear how residues outside the active site modulate the enzymatic activity. To tackle this question, we solved the crystal structure of the GH1 beta-glycosidase from Spodoptera frugiperda (Sfbetagly) to systematically map its residue contact network and correlate effects of mutations within and outside the active site. External mutations neighbouring the functional residues involved in catalysis and glycone-binding are deleterious, whereas mutations neighbouring the aglycone-binding site are less detrimental or even beneficial. The large dataset of new and previously characterized Sfbetagly mutants supports that external perturbations are coherently transmitted to active site residues possibly through contacts and specifically disturb functional regions they interact to, reproducing the effects observed for direct mutations of functional residues. This allowed us to suggest that positions related to the aglycone-binding site are preferential targets for introduction of mutations aiming to further improve the hydrolytic activity of beta-glycosidases. Using the Amino Acid Network to Modulate the Hydrolytic Activity of beta-Glycosidases.,Tamaki FK, Souza DP, Souza VP, Ikegami CM, Farah CS, Marana SR PLoS One. 2016 Dec 9;11(12):e0167978. doi: 10.1371/journal.pone.0167978., eCollection 2016. PMID:27936116 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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