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| | <StructureSection load='7cbd' size='340' side='right'caption='[[7cbd]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='7cbd' size='340' side='right'caption='[[7cbd]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7cbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Celfa Celfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CBD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7cbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellulomonas_fimi_ATCC_484 Cellulomonas fimi ATCC 484]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CBD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbhA, Celf_1925 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=590998 CELFA])</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]] 1.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase_(non-reducing_end) Cellulose 1,4-beta-cellobiosidase (non-reducing end)], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7cbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cbd OCA], [https://pdbe.org/7cbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cbd RCSB], [https://www.ebi.ac.uk/pdbsum/7cbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cbd 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=7cbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cbd OCA], [https://pdbe.org/7cbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cbd RCSB], [https://www.ebi.ac.uk/pdbsum/7cbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cbd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GUXA_CELFA GUXA_CELFA]] This enzyme hydrolyzes 1,4-beta-D-glucosidic linkages of cellulose. Weak activity against carboxymethylcellulose, bacterial microcrystalline cellulose and barley beta-glucan. Has also weak endoglucanase activity. Hydrolyzes glucosidic bonds with inversion of anomeric configuration.
| + | [https://www.uniprot.org/uniprot/GUXA_CELFA GUXA_CELFA] This enzyme hydrolyzes 1,4-beta-D-glucosidic linkages of cellulose. Weak activity against carboxymethylcellulose, bacterial microcrystalline cellulose and barley beta-glucan. Has also weak endoglucanase activity. Hydrolyzes glucosidic bonds with inversion of anomeric configuration. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7cbd" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7cbd" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Celfa]] | + | [[Category: Cellulomonas fimi ATCC 484]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Igarashi, K]] | + | [[Category: Igarashi K]] |
| - | [[Category: Iino, R]] | + | [[Category: Iino R]] |
| - | [[Category: Ishiwata, D]] | + | [[Category: Ishiwata D]] |
| - | [[Category: Kaneko, S]] | + | [[Category: Kaneko S]] |
| - | [[Category: Mizutani, K]] | + | [[Category: Mizutani K]] |
| - | [[Category: Murata, T]] | + | [[Category: Murata T]] |
| - | [[Category: Nakamura, A]] | + | [[Category: Nakamura A]] |
| - | [[Category: Uchiyama, T]] | + | [[Category: Uchiyama T]] |
| - | [[Category: Visootsat, A]] | + | [[Category: Visootsat A]] |
| - | [[Category: Cellulase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
GUXA_CELFA This enzyme hydrolyzes 1,4-beta-D-glucosidic linkages of cellulose. Weak activity against carboxymethylcellulose, bacterial microcrystalline cellulose and barley beta-glucan. Has also weak endoglucanase activity. Hydrolyzes glucosidic bonds with inversion of anomeric configuration.
Publication Abstract from PubMed
Cellobiohydrolases directly convert crystalline cellulose into cellobiose and are of biotechnological interest to achieve efficient biomass utilization. As a result, much research in the field has focused on identifying cellobiohydrolases that are very fast. Cellobiohydrolase A from the bacterium Cellulomonas fimi (CfCel6B) and cellobiohydrolase II from the fungus Trichoderma reesei (TrCel6A) have similar catalytic domains (CDs) and show similar hydrolytic activity. However, TrCel6A and CfCel6B have different cellulose-binding domains (CBDs) and linkers: TrCel6A has a glycosylated peptide linker, whereas CfCel6B's linker consists of three fibronectin type 3 domains. We previously found that TrCel6A's linker plays an important role in increasing the binding rate constant to crystalline cellulose. However, it was not clear whether CfCel6B's linker has similar function. Here we analyze kinetic parameters of CfCel6B using single-molecule fluorescence imaging to compare CfCel6B and TrCel6A. We find that CBD is important for initial binding of CfCel6B, but the contribution of the linker to the binding rate constant or to the dissociation rate constant is minor. The crystal structure of the CfCel6B CD showed longer loops at the entrance and exit of the substrate-binding tunnel compared with TrCel6A CD, which results in higher processivity. Furthermore, CfCel6B CD showed not only fast surface diffusion but also slow processive movement, which is not observed in TrCel6A CD. Combined with the results of a phylogenetic tree analysis, we propose that bacterial cellobiohydrolases are designed to degrade crystalline cellulose using high-affinity CBD and high-processivity CD.
Domain architecture divergence leads to functional divergence in binding and catalytic domains of bacterial and fungal cellobiohydrolases.,Nakamura A, Ishiwata D, Visootsat A, Uchiyama T, Mizutani K, Kaneko S, Murata T, Igarashi K, Iino R J Biol Chem. 2020 Oct 23;295(43):14606-14617. doi: 10.1074/jbc.RA120.014792. Epub, 2020 Aug 18. PMID:32816991[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nakamura A, Ishiwata D, Visootsat A, Uchiyama T, Mizutani K, Kaneko S, Murata T, Igarashi K, Iino R. Domain architecture divergence leads to functional divergence in binding and catalytic domains of bacterial and fungal cellobiohydrolases. J Biol Chem. 2020 Oct 23;295(43):14606-14617. doi: 10.1074/jbc.RA120.014792. Epub, 2020 Aug 18. PMID:32816991 doi:http://dx.doi.org/10.1074/jbc.RA120.014792
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