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| | <StructureSection load='5ju6' size='340' side='right'caption='[[5ju6]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5ju6' size='340' side='right'caption='[[5ju6]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ju6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16479 Atcc 16479]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d0j 4d0j]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JU6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JU6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ju6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rasamsonia_emersonii Rasamsonia emersonii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d0j 4d0j]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JU6 FirstGlance]. <br> |
| - | </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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=5ju6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ju6 OCA], [http://pdbe.org/5ju6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ju6 RCSB], [http://www.ebi.ac.uk/pdbsum/5ju6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ju6 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=5ju6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ju6 OCA], [https://pdbe.org/5ju6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ju6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ju6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ju6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8TGI8_TALEM Q8TGI8_TALEM] |
| | <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: Atcc 16479]] | |
| - | [[Category: Beta-glucosidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gudmundsson, M]] | + | [[Category: Rasamsonia emersonii]] |
| - | [[Category: Karkehabadi, S]] | + | [[Category: Gudmundsson M]] |
| - | [[Category: Sandgren, M]]
| + | [[Category: Karkehabadi S]] |
| - | [[Category: Glycoprotein]] | + | [[Category: Sandgren M]] |
| - | [[Category: Hydrolase]] | + | |
| Structural highlights
5ju6 is a 4 chain structure with sequence from Rasamsonia emersonii. This structure supersedes the now removed PDB entry 4d0j. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q8TGI8_TALEM
Publication Abstract from PubMed
The filamentous fungus Hypocrea jecorina produces a number of cellulases and hemicellulases that act in a concerted fashion on biomass and degrade it into monomeric or oligomeric sugars. beta-Glucosidases are involved in the last step of the degradation of cellulosic biomass and hydrolyse the beta-glycosidic linkage between two adjacent molecules in dimers and oligomers of glucose. In this study, it is shown that substituting the beta-glucosidase from H. jecorina (HjCel3A) with the beta-glucosidase Cel3A from the thermophilic fungus Rasamsonia emersonii (ReCel3A) in enzyme mixtures results in increased efficiency in the saccharification of lignocellulosic materials. Biochemical characterization of ReCel3A, heterologously produced in H. jecorina, reveals a preference for disaccharide substrates over longer gluco-oligosaccharides. Crystallographic studies of ReCel3A revealed a highly N-glycosylated three-domain dimeric protein, as has been observed previously for glycoside hydrolase family 3 beta-glucosidases. The increased thermal stability and saccharification yield and the superior biochemical characteristics of ReCel3A compared with HjCel3A and mixtures containing HjCel3A make ReCel3A an excellent candidate for addition to enzyme mixtures designed to operate at higher temperatures.
Structural and functional studies of the glycoside hydrolase family 3 beta-glucosidase Cel3A from the moderately thermophilic fungus Rasamsonia emersonii.,Gudmundsson M, Hansson H, Karkehabadi S, Larsson A, Stals I, Kim S, Sunux S, Fujdala M, Larenas E, Kaper T, Sandgren M Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):860-70. doi:, 10.1107/S2059798316008482. Epub 2016 Jun 23. PMID:27377383[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gudmundsson M, Hansson H, Karkehabadi S, Larsson A, Stals I, Kim S, Sunux S, Fujdala M, Larenas E, Kaper T, Sandgren M. Structural and functional studies of the glycoside hydrolase family 3 beta-glucosidase Cel3A from the moderately thermophilic fungus Rasamsonia emersonii. Acta Crystallogr D Struct Biol. 2016 Jul 1;72(Pt 7):860-70. doi:, 10.1107/S2059798316008482. Epub 2016 Jun 23. PMID:27377383 doi:http://dx.doi.org/10.1107/S2059798316008482
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