5ju6
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/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> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:27377383</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5ju6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:05, 27 July 2016
Structural and Functional Studies of Glycoside Hydrolase Family 3 beta-Glucosidase Cel3A from the Moderately Thermophilic Fungus Rasamsonia emersonii
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