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| | ==Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3== | | ==Solution structure of the Family 1 carbohydrate-binding module Y5A mutant with mannosylated Ser3== |
| - | <StructureSection load='5x3c' size='340' side='right'caption='[[5x3c]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='5x3c' size='340' side='right'caption='[[5x3c]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x3c]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X3C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X3C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x3c]] 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=5X3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X3C FirstGlance]. <br> |
| | </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> | | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x34|5x34]], [[5x35|5x35]], [[5x36|5x36]], [[5x37|5x37]], [[5x38|5x38]], [[5x39|5x39]]</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=5x3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x3c OCA], [https://pdbe.org/5x3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x3c RCSB], [https://www.ebi.ac.uk/pdbsum/5x3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x3c ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x3c OCA], [http://pdbe.org/5x3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x3c RCSB], [http://www.ebi.ac.uk/pdbsum/5x3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x3c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Feng, Y]] | + | [[Category: Trichoderma reesei]] |
| - | [[Category: Tan, Z]] | + | [[Category: Feng Y]] |
| - | [[Category: Carbohydrate binding]] | + | [[Category: Tan Z]] |
| - | [[Category: Hydrolase]]
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| Structural highlights
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
Protein glycosylation has been shown to have a variety of site-specific and glycan-specific effects, but so far, the molecular logic that leads to such observations has been elusive. Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to predict how specific glycosylation patterns will affect the stability of glycoproteins. By systematically comparing the structural features of the O-glycosylated carbohydrate-binding module of a Trichoderma reesei-derived Family 7 cellobiohydrolase, we were able to develop a better understanding of the influence of O-glycan structure on the molecule's physical stability. Our results indicate that the previously observed stabilizing effects of O-glycans come from the introduction of new bonding interactions to the structure and increased rigidity, while the decreased stability seemed to result from the impaired interactions and increased conformational flexibility. This type of knowledge provides a powerful and potentially general mechanism for improving the stability of proteins through glycoengineering.
Structural Insight into the Stabilizing Effect of O-Glycosylation.,Chaffey PK, Guan X, Chen C, Ruan Y, Wang X, Tran AH, Koelsch TN, Cui Q, Feng Y, Tan Z Biochemistry. 2017 Jun 13;56(23):2897-2906. doi: 10.1021/acs.biochem.7b00195., Epub 2017 Jun 1. PMID:28494147[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chaffey PK, Guan X, Chen C, Ruan Y, Wang X, Tran AH, Koelsch TN, Cui Q, Feng Y, Tan Z. Structural Insight into the Stabilizing Effect of O-Glycosylation. Biochemistry. 2017 Jun 13;56(23):2897-2906. doi: 10.1021/acs.biochem.7b00195., Epub 2017 Jun 1. PMID:28494147 doi:http://dx.doi.org/10.1021/acs.biochem.7b00195
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