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| | ==The structure of WT Bgl6== | | ==The structure of WT Bgl6== |
| - | <StructureSection load='5gny' size='340' side='right' caption='[[5gny]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5gny' size='340' side='right'caption='[[5gny]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gny]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GNY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GNY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gny]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Metagenome Metagenome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GNY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GNY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</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]] 2.105Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gnx|5gnx]], [[5gnz|5gnz]]</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </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=5gny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gny OCA], [https://pdbe.org/5gny PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gny RCSB], [https://www.ebi.ac.uk/pdbsum/5gny PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gny ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gny FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gny OCA], [http://pdbe.org/5gny PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gny RCSB], [http://www.ebi.ac.uk/pdbsum/5gny PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gny ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-glucosidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Cao, L C]] | + | [[Category: Metagenome]] |
| - | [[Category: Liu, Y H]] | + | [[Category: Cao LC]] |
| - | [[Category: Pang, P]] | + | [[Category: Liu YH]] |
| - | [[Category: Wang, Z]] | + | [[Category: Pang P]] |
| - | [[Category: Xie, W]] | + | [[Category: Wang Z]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Xie W]] |
| - | [[Category: Tim-barrel fold]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Cellulose can be converted to ethanol via the fermentation of glucose, which is considered as a promising green alternative for transportation fuels. The conversion of cellulose to glucose needs three enzymes, in which beta-glucosidase (BGL) plays an essential role. However, BGL is inhibited by its own product glucose, greatly limiting its applications in industry. We previously obtained a novel BGL named Bgl6 with a high glucose tolerance. Further engineering through random mutagenesis produced a triple mutant M3 with improved thermostability. This enzyme shows promising properties for wide applications but the structural basis of the unusual properties of Bgl6 is not clear. In this study, we determined the crystal structures of Bgl6 and variants at high resolution, which provide insights into its glucose-tolerant mechanism and thermostability. Particularly, Bgl6 forms an extra channel that could be used as a secondary binding site for glucose, which may contribute to glucose tolerance. Additionally, the triple mutations could strengthen the hydrophobic interactions within the enzyme and may be responsible for the enhanced thermostability exhibited by M3, which was further confirmed by dynamic light scattering data. Lastly, structural comparison to other orthologs allows us to formulate new strategies on how to improve the catalytic efficiency of Bgl6.
Structures of a glucose-tolerant beta-glucosidase provide insights into its mechanism.,Pang P, Cao LC, Liu YH, Xie W, Wang Z J Struct Biol. 2017 Feb 9. pii: S1047-8477(17)30017-5. doi:, 10.1016/j.jsb.2017.02.001. PMID:28189793[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pang P, Cao LC, Liu YH, Xie W, Wang Z. Structures of a glucose-tolerant beta-glucosidase provide insights into its mechanism. J Struct Biol. 2017 Feb 9. pii: S1047-8477(17)30017-5. doi:, 10.1016/j.jsb.2017.02.001. PMID:28189793 doi:http://dx.doi.org/10.1016/j.jsb.2017.02.001
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