7f3a: Difference between revisions
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==Arabidopsis thaliana GH1 beta-glucosidase AtBGlu42== | ==Arabidopsis thaliana GH1 beta-glucosidase AtBGlu42== | ||
<StructureSection load='7f3a' size='340' side='right'caption='[[7f3a]]' scene=''> | <StructureSection load='7f3a' size='340' side='right'caption='[[7f3a]], [[Resolution|resolution]] 1.70Å' 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=7F3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F3A FirstGlance]. <br> | <table><tr><td colspan='2'>[[7f3a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7F3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7F3A 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=7f3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f3a OCA], [https://pdbe.org/7f3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f3a RCSB], [https://www.ebi.ac.uk/pdbsum/7f3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f3a 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]] 1.7Å</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=7f3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7f3a OCA], [https://pdbe.org/7f3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7f3a RCSB], [https://www.ebi.ac.uk/pdbsum/7f3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7f3a ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/BGL42_ARATH BGL42_ARATH] Glucosidase that hydrolyzes scopolin and various beta-glucosides, cellooligosaccharides (mainly cellotriose) and laminarioligosaccharides (PubMed:34965581). Can use p-nitrophenyl-beta-glucosides (pNP beta-Glc) and p-nitrophenyl-beta-D-fucosides (pNP beta-D-Fuc) as substrates, and, to a lower extent, beta-galactosides, beta-mannosides and beta-xylosides (PubMed:34965581). Involved in the secretion of root-derived phenolics upon iron ions (Fe) depletion (PubMed:25138267). Promotes disease resistance toward B.cinerea, H.arabidopsidis and P.syringae pv. tomato DC3000 (PubMed:25138267). Required during rhizobacteria-mediated (e.g. P.fluorescens WCS417r) broad-spectrum induced systemic resistance (ISR) against several pathogens (PubMed:25138267).<ref>PMID:25138267</ref> <ref>PMID:34965581</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plants possess many glycoside hydrolase family 1 (GH1) beta-glucosidases, which physiologically function in cell wall metabolism and activation of bioactive substances, but most remain uncharacterized. One GH1 isoenzyme AtBGlu42 in Arabidopsis thaliana has been identified to hydrolyze scopolin using the gene deficient plants, but no enzymatic properties were obtained. Its sequence similarity to another functionally characterized enzyme Os1BGlu4 in rice suggests that AtBGlu42 also acts on oligosaccharides. Here, we show that the recombinant AtBGlu42 possesses high kcat/Km not only on scopolin, but also on various beta-glucosides, cellooligosaccharides, and laminarioligosaccharides. Of the cellooligosaccharides, cellotriose was the most preferred. The crystal structure, determined at 1.7 A resolution, suggests that Arg342 gives unfavorable binding to cellooligosaccharides at subsite +3. The mutants R342Y and R342A showed the highest preference on cellotetraose or cellopentaose with increased affinities at subsite +3, indicating that the residues at this position have an important role for chain length specificity. | |||
Substrate specificity of glycoside hydrolase family 1 beta-glucosidase AtBGlu42 from Arabidopsis thaliana and its molecular mechanism.,Horikoshi S, Saburi W, Yu J, Matsuura H, Cairns JRK, Yao M, Mori H Biosci Biotechnol Biochem. 2022 Jan 24;86(2):231-245. doi: 10.1093/bbb/zbab200. PMID:34965581<ref>PMID:34965581</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7f3a" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Horikoshi S]] | [[Category: Horikoshi S]] | ||
Latest revision as of 20:08, 29 November 2023
Arabidopsis thaliana GH1 beta-glucosidase AtBGlu42Arabidopsis thaliana GH1 beta-glucosidase AtBGlu42
Structural highlights
FunctionBGL42_ARATH Glucosidase that hydrolyzes scopolin and various beta-glucosides, cellooligosaccharides (mainly cellotriose) and laminarioligosaccharides (PubMed:34965581). Can use p-nitrophenyl-beta-glucosides (pNP beta-Glc) and p-nitrophenyl-beta-D-fucosides (pNP beta-D-Fuc) as substrates, and, to a lower extent, beta-galactosides, beta-mannosides and beta-xylosides (PubMed:34965581). Involved in the secretion of root-derived phenolics upon iron ions (Fe) depletion (PubMed:25138267). Promotes disease resistance toward B.cinerea, H.arabidopsidis and P.syringae pv. tomato DC3000 (PubMed:25138267). Required during rhizobacteria-mediated (e.g. P.fluorescens WCS417r) broad-spectrum induced systemic resistance (ISR) against several pathogens (PubMed:25138267).[1] [2] Publication Abstract from PubMedPlants possess many glycoside hydrolase family 1 (GH1) beta-glucosidases, which physiologically function in cell wall metabolism and activation of bioactive substances, but most remain uncharacterized. One GH1 isoenzyme AtBGlu42 in Arabidopsis thaliana has been identified to hydrolyze scopolin using the gene deficient plants, but no enzymatic properties were obtained. Its sequence similarity to another functionally characterized enzyme Os1BGlu4 in rice suggests that AtBGlu42 also acts on oligosaccharides. Here, we show that the recombinant AtBGlu42 possesses high kcat/Km not only on scopolin, but also on various beta-glucosides, cellooligosaccharides, and laminarioligosaccharides. Of the cellooligosaccharides, cellotriose was the most preferred. The crystal structure, determined at 1.7 A resolution, suggests that Arg342 gives unfavorable binding to cellooligosaccharides at subsite +3. The mutants R342Y and R342A showed the highest preference on cellotetraose or cellopentaose with increased affinities at subsite +3, indicating that the residues at this position have an important role for chain length specificity. Substrate specificity of glycoside hydrolase family 1 beta-glucosidase AtBGlu42 from Arabidopsis thaliana and its molecular mechanism.,Horikoshi S, Saburi W, Yu J, Matsuura H, Cairns JRK, Yao M, Mori H Biosci Biotechnol Biochem. 2022 Jan 24;86(2):231-245. doi: 10.1093/bbb/zbab200. PMID:34965581[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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