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| | <StructureSection load='6sz6' size='340' side='right'caption='[[6sz6]], [[Resolution|resolution]] 2.99Å' scene=''> | | <StructureSection load='6sz6' size='340' side='right'caption='[[6sz6]], [[Resolution|resolution]] 2.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sz6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SZ6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SZ6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sz6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SZ6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.988Å</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=6sz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sz6 OCA], [http://pdbe.org/6sz6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sz6 RCSB], [http://www.ebi.ac.uk/pdbsum/6sz6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sz6 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6sz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sz6 OCA], [https://pdbe.org/6sz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sz6 RCSB], [https://www.ebi.ac.uk/pdbsum/6sz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sz6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A6YRT4_9PEZI A6YRT4_9PEZI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 144 50]] | + | [[Category: Chaetomium thermophilum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mohsin, I]] | + | [[Category: Mohsin I]] |
| - | [[Category: Papageorgiou, A C]] | + | [[Category: Papageorgiou AC]] |
| - | [[Category: Poudel, N]] | + | [[Category: Poudel N]] |
| - | [[Category: Biofuel]]
| + | |
| - | [[Category: Cellulose degradation]]
| + | |
| - | [[Category: Glucosidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Thermophilic fungus]]
| + | |
| Structural highlights
Function
A6YRT4_9PEZI
Publication Abstract from PubMed
Beta-glucosidases (beta-glucosidases) have attracted considerable attention in recent years for use in various biotechnological applications. They are also essential enzymes for lignocellulose degradation in biofuel production. However, cost-effective biomass conversion requires the use of highly efficient enzymes. Thus, the search for new enzymes as better alternatives of the currently available enzyme preparations is highly important. Thermophilic fungi are nowadays considered as a promising source of enzymes with improved stability. Here, the crystal structure of a family GH3 beta-glucosidase from the thermophilic fungus Chaetomium thermophilum (CtBGL) was determined at a resolution of 2.99 A. The structure showed the three-domain architecture found in other beta-glucosidases with variations in loops and linker regions. The active site catalytic residues in CtBGL were identified as Asp287 (nucleophile) and Glu517 (acid/base). Structural comparison of CtBGL with Protein Data Bank (PDB)-deposited structures revealed variations among glycosylated Asn residues. The enzyme displayed moderate glycosylation compared to other GH3 family beta-glucosidases with similar structure. A new glycosylation site at position Asn504 was identified in CtBGL. Moreover, comparison with respect to several thermostability parameters suggested that glycosylation and charged residues involved in electrostatic interactions may contribute to the stability of the enzyme at elevated temperatures. The reported CtBGL structure provides additional insights into the family GH3 enzymes and could offer new ideas for further improvements in beta-glucosidases for more efficient use in biotechnological applications regarding cellulose degradation.
Crystal Structure of a GH3 beta-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum.,Mohsin I, Poudel N, Li DC, Papageorgiou AC Int J Mol Sci. 2019 Nov 27;20(23). pii: ijms20235962. doi: 10.3390/ijms20235962. PMID:31783503[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mohsin I, Poudel N, Li DC, Papageorgiou AC. Crystal Structure of a GH3 beta-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum. Int J Mol Sci. 2019 Nov 27;20(23). pii: ijms20235962. doi: 10.3390/ijms20235962. PMID:31783503 doi:http://dx.doi.org/10.3390/ijms20235962
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