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| | <StructureSection load='5gm5' size='340' side='right'caption='[[5gm5]], [[Resolution|resolution]] 1.73Å' scene=''> | | <StructureSection load='5gm5' size='340' side='right'caption='[[5gm5]], [[Resolution|resolution]] 1.73Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gm5]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspac Aspac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GM5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GM5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gm5]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GM5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.73Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gm4|5gm4]], [[5gm3|5gm3]]</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=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=5gm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gm5 OCA], [https://pdbe.org/5gm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gm5 RCSB], [https://www.ebi.ac.uk/pdbsum/5gm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gm5 ProSAT]</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=5gm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gm5 OCA], [http://pdbe.org/5gm5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gm5 RCSB], [http://www.ebi.ac.uk/pdbsum/5gm5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gm5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/GUN_ASPAC GUN_ASPAC] |
| | <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: Aspac]] | + | [[Category: Aspergillus aculeatus]] |
| - | [[Category: Cellulase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, C C]] | + | [[Category: Chen CC]] |
| - | [[Category: Guo, R T]] | + | [[Category: Guo RT]] |
| - | [[Category: Huang, J W]] | + | [[Category: Huang JW]] |
| - | [[Category: Liu, W D]] | + | [[Category: Liu WD]] |
| - | [[Category: Zheng, Y Y]] | + | [[Category: Zheng YY]] |
| - | [[Category: Hydrolase-inhibitor complex]]
| + | |
| - | [[Category: Substrate binding]]
| + | |
| Structural highlights
Function
GUN_ASPAC
Publication Abstract from PubMed
Cellulose is the major component of the plant cell wall and the most abundant renewable biomass on earth, and its decomposition has proven to be very useful in many commercial applications. Endo-1,4-beta-d-glucanase (EC 3.2.1.4; endoglucanase), which catalyzes the random hydrolysis of 1,4-beta-glycosidic bonds of the cellulose main chain to cleave cellulose into smaller fragments, is the key cellulolytic enzyme. An endoglucanase isolated from Aspergillus aculeatus F-50 (FI-CMCase), which is classified into the glycoside hydrolase (GH) family 12, was demonstrated to be effectively expressed in the industrial strain Pichia pastoris. Here, the crystal structure and complex structures of P. pastoris-expressed FI-CMCase were solved to high resolution. The overall structure is analyzed and compared to other GH12 members. In addition, the substrate-surrounding residues were engineered to search for variants with improved enzymatic activity. Among 14 mutants constructed, one with two-fold increase in protein expression was identified, which possesses a potential to be further developed as a commercial enzyme product.
Crystal structure and genetic modifications of FI-CMCase from Aspergillus aculeatus F-50.,Huang JW, Liu W, Lai HL, Cheng YS, Zheng Y, Li Q, Sun H, Kuo CJ, Guo RT, Chen CC Biochem Biophys Res Commun. 2016 Sep 16;478(2):565-72. doi:, 10.1016/j.bbrc.2016.07.101. Epub 2016 Jul 25. PMID:27470581[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huang JW, Liu W, Lai HL, Cheng YS, Zheng Y, Li Q, Sun H, Kuo CJ, Guo RT, Chen CC. Crystal structure and genetic modifications of FI-CMCase from Aspergillus aculeatus F-50. Biochem Biophys Res Commun. 2016 Sep 16;478(2):565-72. doi:, 10.1016/j.bbrc.2016.07.101. Epub 2016 Jul 25. PMID:27470581 doi:http://dx.doi.org/10.1016/j.bbrc.2016.07.101
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