7yhh: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7yhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YHH FirstGlance]. <br> | <table><tr><td colspan='2'>[[7yhh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YHH FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7yhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yhh OCA], [https://pdbe.org/7yhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yhh RCSB], [https://www.ebi.ac.uk/pdbsum/7yhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yhh ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7yhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yhh OCA], [https://pdbe.org/7yhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yhh RCSB], [https://www.ebi.ac.uk/pdbsum/7yhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yhh ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/GUX1_HYPJE 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. | [https://www.uniprot.org/uniprot/GUX1_HYPJE 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. | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:37666405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7yhh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 09:57, 21 November 2024
Solution structure of S-di-mannosylated S3C mutant of carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reeseiSolution structure of S-di-mannosylated S3C mutant of carbohydrate binding module (CBM) of the glycoside hydrolase Family 7 cellobiohydrolase from Trichoderma reesei
Structural highlights
FunctionGUX1_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 PubMedThere 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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