7yhh | pdb_00007yhh

Solution structure of S-di-mannosylated S3C mutant of carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reesei

spinqualitylabelsall models 7yhh Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7yhh is a 1 chain structure with sequence from Trichoderma reesei. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Ligands: MAN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GUX1_HYPJE The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose. Publication Abstract from PubMed There is an increasing interest in using S-glycosylation as a replacement for the more commonly occurring O-glycosylation, aiming to enhance the resistance of glycans against chemical hydrolysis and enzymatic degradation. However, previous studies have demonstrated that these two types of glycosylation exert distinct effects on protein properties and functions. In order to elucidate the structural basis behind the observed differences, we conducted a systematic and comparative analysis of 6 differently glycosylated forms of a model glycoprotein, CBM, using NMR spectroscopy and molecular dynamic simulations. Our findings revealed that the different stabilizing effects of S- and O-glycosylation could be attributed to altered hydrogen-bonding capability between the glycan and the polypeptide chain, and their diverse impacts on binding affinity could be elucidated by examining the interactions and motion dynamics of glycans in substrate-bound states. Overall, this study underscores the pivotal role of the glycosidic linkage in shaping the function of glycosylation and advises caution when switching glycosylation types in protein glycoengineering. Structural insight into why S-linked glycosylation cannot adequately mimic the role of natural O-glycosylation.,Chen C, Ma B, Wang Y, Cui Q, Yao L, Li Y, Chen B, Feng Y, Tan Z Int J Biol Macromol. 2023 Dec 31;253(Pt 1):126649. doi: , 10.1016/j.ijbiomac.2023.126649. Epub 2023 Sep 2. PMID:37666405 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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