8akp | pdb_00008akp

Crystal structure of the catalytic domain of G7048 from Penicillium sumatraense

spinqualitylabelsall models 8akp, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8akp is a 1 chain structure with sequence from Penicillium sumatraense. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BMA, MAN, NAG, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed BACKGROUND: 1,3-beta-glucan is a polysaccharide widely distributed in the cell wall of several phylogenetically distant organisms, such as bacteria, fungi, plants and microalgae. The presence of highly active 1,3-beta-glucanases in fungi evokes the biological question on how these organisms can efficiently metabolize exogenous sources of 1,3-beta-glucan without incurring in autolysis. RESULTS: To elucidate the molecular mechanisms at the basis of 1,3-beta-glucan metabolism in fungal saprotrophs, the putative exo-1,3-beta-glucanase G9376 and a truncated form of the putative glucan endo-1,3-beta-glucosidase (DeltaG7048) from Penicillium sumatraense AQ67100 were heterologously expressed in Pichia pastoris and characterized both in terms of activity and structure. G9376 efficiently converted laminarin and 1,3-beta-glucan oligomers into glucose by acting as an exo-glycosidase, whereas G7048 displayed a 1,3-beta-transglucanase/branching activity toward 1,3-beta-glucan oligomers with a degree of polymerization higher than 5, making these oligomers more recalcitrant to the hydrolysis acted by exo-1,3-beta-glucanase G9376. The X-ray crystallographic structure of the catalytic domain of G7048, solved at 1.9 A of resolution, consists of a (beta/alpha)(8) TIM-barrel fold characteristic of all the GH17 family members. The catalytic site is in a V-shaped cleft containing the two conserved catalytic glutamic residues. Molecular features compatible with the activity of G7048 as 1,3-beta-transglucanase are discussed. CONCLUSIONS: The antagonizing activity between DeltaG7048 and G9376 indicates how opportunistic fungi belonging to Penicillium genus can feed on substrates similar for composition and structure to their own cell wall without incurring in a self-deleterious autohydrolysis. Characterization of two 1,3-beta-glucan-modifying enzymes from Penicillium sumatraense reveals new insights into 1,3-beta-glucan metabolism of fungal saprotrophs.,Scafati V, Troilo F, Ponziani S, Giovannoni M, Scortica A, Pontiggia D, Angelucci F, Di Matteo A, Mattei B, Benedetti M Biotechnol Biofuels Bioprod. 2022 Dec 12;15(1):138. doi: , 10.1186/s13068-022-02233-8. PMID:36510318 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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