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| <StructureSection load='7ee2' size='340' side='right'caption='[[7ee2]], [[Resolution|resolution]] 1.37Å' scene=''> | | <StructureSection load='7ee2' size='340' side='right'caption='[[7ee2]], [[Resolution|resolution]] 1.37Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7ee2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EE2 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EE2 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.3701164Å</td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] </span></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7ee2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ee2 OCA], [https://pdbe.org/7ee2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ee2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ee2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ee2 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=7ee2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ee2 OCA], [https://pdbe.org/7ee2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ee2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ee2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ee2 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| beta-1,3-1,4-Glucanases are a type of hydrolytic enzymes capable of catalyzing the strict cleavage of beta-1,4 glycosidic bonds adjacent to beta-1,3 linkages in beta-D-glucans and have exhibited great potential in food and feed industrials. In this study, a novel glycoside hydrolase (GH) family 12 beta-1,3-1,4-glucanase (CtGlu12A) from the thermophilic fungus Chaetomium sp. CQ31 was identified and biochemically characterized. CtGlu12A was most active at pH 7.5 and 65 degrees C, respectively, and exhibited a high specific activity of 999.9 U mg(-1) towards lichenin. It maintained more than 80% of its initial activity in a wide pH range of 5.0-11.0, and up to 60 degrees C after incubation at 55 degrees C for 60 min. Moreover, the crystal structures of CtGlu12A with gentiobiose and tetrasccharide were resolved. CtGlu12A had a beta-jellyroll fold, and performed retaining mechanism with two glutamic acids severing as the catalytic residues. In the complex structure, cellobiose molecule showed two binding modes, occupying subsites -2 to -1 and subsites + 1 to + 2, respectively. The concave cleft made mixed beta-1,3-1,4-glucan substrates maintain a bent conformation to fit into the active site. Overall, this study is not only helpful for the understanding of the substrate-binding model and catalytic mechanism of GH 12 beta-1,3-1,4-glucanases, but also provides a basis for further enzymatic engineering of beta-1,3-1,4-glucanases.
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| Structural and biochemical insights into the substrate-binding mechanism of a glycoside hydrolase family 12 beta-1,3-1,4-glucanase from Chaetomium sp.,Ma J, Li Y, Han S, Jiang Z, Yan Q, Yang S J Struct Biol. 2021 Sep;213(3):107774. doi: 10.1016/j.jsb.2021.107774. Epub 2021 , Jul 27. PMID:34329700<ref>PMID:34329700</ref>
| | ==See Also== |
| | | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7ee2" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Licheninase]]
| | [[Category: Jiang ZQ]] |
| [[Category: Jiang, Z Q]] | | [[Category: Ma J]] |
| [[Category: Ma, J]] | |
| [[Category: 3-1]]
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| [[Category: 4-glucanase]]
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| [[Category: Beta-1]]
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| [[Category: Catalytic mechanism]]
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| [[Category: Hydrolase]]
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| [[Category: Structural protein]]
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| [[Category: Substrate binding]]
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