3wh5: Difference between revisions
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==Crystal structure of GH1 beta-glucosidase Td2F2== | ==Crystal structure of GH1 beta-glucosidase Td2F2== | ||
<StructureSection load='3wh5' size='340' side='right'caption='[[3wh5]]' scene=''> | <StructureSection load='3wh5' size='340' side='right'caption='[[3wh5]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WH5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3wh5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Metagenomes Metagenomes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WH5 FirstGlance]. <br> | ||
</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=3wh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wh5 OCA], [https://pdbe.org/3wh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wh5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wh5 ProSAT]</span></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]] 1.6Å</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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=3wh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wh5 OCA], [https://pdbe.org/3wh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wh5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wh5 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-Glucosidase Td2F2 isolated from a compost metagenome has high glucose tolerance and transglycosylation activity. In this study, we determined the high-resolution crystal structure of Td2F2. It has a unique structure at the -1 subsite that is important for substrate specificity but not for glucose tolerance. To elucidate the mechanism(s) of glucose tolerance, we isolated a glucose-sensitive Td2F2 mutant using random mutagenesis. In this mutant, Asn223 residue located between subsites +1 and +2 was mutated. The Asn223 mutation resulted in reduced glucose tolerance and transglycosylation activity, and drastically changed substrate specificity. These results indicate that the structure between subsites +1 and +2 is critical for the glucose tolerance and substrate specificity of Td2F2. Our findings shed light on the glucose tolerance and transglycosylation activity mechanisms of glycoside hydrolase family 1 beta-glucosidases. This article is protected by copyright. All rights reserved. | |||
Crystal structure and identification of a key amino acid for glucose tolerance, substrate specificity and transglycosylation activity of metagenomic beta-glucosidase Td2F2.,Matsuzawa T, Jo T, Uchiyama T, Manninen JA, Arakawa T, Miyazaki K, Fushinobu S, Yaoi K FEBS J. 2016 Apr 19. doi: 10.1111/febs.13743. PMID:27092463<ref>PMID:27092463</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wh5" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Metagenomes]] | |||
[[Category: Fushinobu S]] | [[Category: Fushinobu S]] | ||
[[Category: Jo T]] | [[Category: Jo T]] | ||
[[Category: Uchiyama T]] | [[Category: Uchiyama T]] | ||
[[Category: Yaoi K]] | [[Category: Yaoi K]] | ||
Latest revision as of 16:10, 8 November 2023
Crystal structure of GH1 beta-glucosidase Td2F2Crystal structure of GH1 beta-glucosidase Td2F2
Structural highlights
Publication Abstract from PubMedbeta-Glucosidase Td2F2 isolated from a compost metagenome has high glucose tolerance and transglycosylation activity. In this study, we determined the high-resolution crystal structure of Td2F2. It has a unique structure at the -1 subsite that is important for substrate specificity but not for glucose tolerance. To elucidate the mechanism(s) of glucose tolerance, we isolated a glucose-sensitive Td2F2 mutant using random mutagenesis. In this mutant, Asn223 residue located between subsites +1 and +2 was mutated. The Asn223 mutation resulted in reduced glucose tolerance and transglycosylation activity, and drastically changed substrate specificity. These results indicate that the structure between subsites +1 and +2 is critical for the glucose tolerance and substrate specificity of Td2F2. Our findings shed light on the glucose tolerance and transglycosylation activity mechanisms of glycoside hydrolase family 1 beta-glucosidases. This article is protected by copyright. All rights reserved. Crystal structure and identification of a key amino acid for glucose tolerance, substrate specificity and transglycosylation activity of metagenomic beta-glucosidase Td2F2.,Matsuzawa T, Jo T, Uchiyama T, Manninen JA, Arakawa T, Miyazaki K, Fushinobu S, Yaoi K FEBS J. 2016 Apr 19. doi: 10.1111/febs.13743. PMID:27092463[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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