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| | <StructureSection load='5i79' size='340' side='right'caption='[[5i79]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5i79' size='340' side='right'caption='[[5i79]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i79]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I79 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I79 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i79]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I79 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CTT:BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSYL-(1- 4)-BETA-D-GLUCOPYRANOSE'>CTT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i78|5i78]], [[5i77|5i77]]</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRD_900011:beta-cellotetraose'>PRD_900011</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eg1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5061 A. niger])</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=5i79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i79 OCA], [https://pdbe.org/5i79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i79 RCSB], [https://www.ebi.ac.uk/pdbsum/5i79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i79 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=5i79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i79 OCA], [http://pdbe.org/5i79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i79 RCSB], [http://www.ebi.ac.uk/pdbsum/5i79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i79 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EGLB_ASPNG EGLB_ASPNG] Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.<ref>PMID:16233124</ref> |
| | <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: A. niger]] | + | [[Category: Aspergillus niger]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, C C]] | + | [[Category: Chen CC]] |
| - | [[Category: Guo, R T]] | + | [[Category: Guo RT]] |
| - | [[Category: Li, Y J]] | + | [[Category: Li YJ]] |
| - | [[Category: Liu, W D]] | + | [[Category: Liu WD]] |
| - | [[Category: Yan, J J]] | + | [[Category: Yan JJ]] |
| - | [[Category: Zheng, Y Y]] | + | [[Category: Zheng YY]] |
| - | [[Category: Endoglucanase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Substrate binding]]
| + | |
| Structural highlights
5i79 is a 2 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.35Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
EGLB_ASPNG Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.[1]
Publication Abstract from PubMed
Eukaryotic 1,4-beta-endoglucanases (EC 3.2.1.4) have shown great potentials in many commercial applications because they effectively catalyze hydrolysis of cellulose, the main component of the plant cell wall. Here we expressed a glycoside hydrolase family (GH) 5 1,4-beta-endoglucanase from Aspergillus niger (AnCel5A) in Pichia pastoris, which exhibits outstanding pH and heat stability. In order to further investigate the molecular mechanism of AnCel5A, apo-form and cellotetraose (CTT) complex enzyme crystal structures were solved to high resolution. AnCel5A folds into a typical (beta/alpha)8-TIM barrel architecture, resembling other GH5 members. In the substrate binding cavity, CTT is found to bind to -4 - -1 subsites, and several polyethylene glycol molecules are found in positive subsites. In addition, several unique N-glycosylation motifs that may contribute to protein higher stability were observed from crystal structures. These results are of great importance for understanding the molecular mechanism of AnCel5A, and also provide guidance for further applications of the enzyme.
Functional and structural analysis of Pichia pastoris-expressed Aspergillus niger 1,4-beta-endoglucanase.,Yan J, Liu W, Li Y, Lai HL, Zheng Y, Huang JW, Chen CC, Chen Y, Jin J, Li H, Guo RT Biochem Biophys Res Commun. 2016 Jun 17;475(1):8-12. doi:, 10.1016/j.bbrc.2016.05.012. Epub 2016 May 3. PMID:27154222[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hong J, Tamaki H, Akiba S, Yamamoto K, Kumagai H. Cloning of a gene encoding a highly stable endo-beta-1,4-glucanase from Aspergillus niger and its expression in yeast. J Biosci Bioeng. 2001;92(5):434-41. PMID:16233124 doi:10.1263/jbb.92.434
- ↑ Yan J, Liu W, Li Y, Lai HL, Zheng Y, Huang JW, Chen CC, Chen Y, Jin J, Li H, Guo RT. Functional and structural analysis of Pichia pastoris-expressed Aspergillus niger 1,4-beta-endoglucanase. Biochem Biophys Res Commun. 2016 Jun 17;475(1):8-12. doi:, 10.1016/j.bbrc.2016.05.012. Epub 2016 May 3. PMID:27154222 doi:http://dx.doi.org/10.1016/j.bbrc.2016.05.012
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