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| | <StructureSection load='4v20' size='340' side='right'caption='[[4v20]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4v20' size='340' side='right'caption='[[4v20]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v20]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V20 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V20 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v20]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V20 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=U63:2-DEOXY-2-FLUORO-4-O-BETA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSE'>U63</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900082:2-deoxy-2-fluoro-beta-D-cellobiose'>PRD_900082</scene>, <scene name='pdbligand=SHG:2-DEOXY-2-FLUORO-BETA-D-GLUCOPYRANOSE'>SHG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=4v20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v20 OCA], [https://pdbe.org/4v20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v20 RCSB], [https://www.ebi.ac.uk/pdbsum/4v20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v20 ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v1z|4v1z]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4v20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v20 OCA], [http://pdbe.org/4v20 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v20 RCSB], [http://www.ebi.ac.uk/pdbsum/4v20 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v20 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CBHB_ASPFU CBHB_ASPFU]] 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/CBHB_ASPFU CBHB_ASPFU] 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspfm]] | + | [[Category: Aspergillus fumigatus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davies, G J]] | + | [[Category: Davies GJ]] |
| - | [[Category: Harris, P V]] | + | [[Category: Harris PV]] |
| - | [[Category: Maranta, M]] | + | [[Category: Maranta M]] |
| - | [[Category: Moroz, O V]] | + | [[Category: Moroz OV]] |
| - | [[Category: Shaghasi, T]] | + | [[Category: Shaghasi T]] |
| - | [[Category: Wilson, K S]] | + | [[Category: Wilson KS]] |
| - | [[Category: Biofuel]]
| + | |
| - | [[Category: Carbohydrate-active enzyme]]
| + | |
| - | [[Category: Cellulase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Thermal stability]]
| + | |
| Structural highlights
4v20 is a 1 chain structure with sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CBHB_ASPFU 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
The enzymatic degradation of plant cell-wall cellulose is central to many industrial processes, including second-generation biofuel production. Key players in this deconstruction are the fungal cellobiohydrolases (CBHs), notably those from family GH7 of the carbohydrate-active enzymes (CAZY) database, which are generally known as CBHI enzymes. Here, three-dimensional structures are reported of the Aspergillus fumigatus CBHI Cel7A solved in uncomplexed and disaccharide-bound forms at resolutions of 1.8 and 1.5 A, respectively. The product complex with a disaccharide in the +1 and +2 subsites adds to the growing three-dimensional insight into this family of industrially relevant biocatalysts.
The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 A resolution.,Moroz OV, Maranta M, Shaghasi T, Harris PV, Wilson KS, Davies GJ Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):114-20. doi:, 10.1107/S2053230X14027307. Epub 2015 Jan 1. PMID:25615982[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Moroz OV, Maranta M, Shaghasi T, Harris PV, Wilson KS, Davies GJ. The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 A resolution. Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):114-20. doi:, 10.1107/S2053230X14027307. Epub 2015 Jan 1. PMID:25615982 doi:http://dx.doi.org/10.1107/S2053230X14027307
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