3aiu: Difference between revisions
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==Crystal structure of beta-glucosidase in rye== | |||
<StructureSection load='3aiu' size='340' side='right'caption='[[3aiu]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3aiu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Secale_cereale Secale cereale]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AIU FirstGlance]. <br> | |||
</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3aiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aiu OCA], [https://pdbe.org/3aiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aiu RCSB], [https://www.ebi.ac.uk/pdbsum/3aiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aiu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HGGL_SECCE HGGL_SECCE] Involved in defense of young plant parts against pests via the production of benzoxazolinones (hydroxamic acids) from hydroxamic acid glucosides. The preferred substrate is DIBOA-beta-D-glucoside. Can also use esculin and genistein glucoside as substrates, but no activity with salicin, p-nitrophenyl-alpha-glucoside or substrates related to cell wall components.<ref>PMID:10773341</ref> [PDB:3AIU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The beta-D-glucosidases from wheat (Triticum aestivum) and rye (Secale cereale) hydrolyze benzoxazinone-glucose conjugates. Although wheat and rye glucosidases have high sequence identity, they have different substrate preferences; the wheat enzyme favors DIMBOA-Glc (2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one) over DIBOA-Glc (7-demethoxy-DIMBOA-Glc), whereas the rye enzyme preference is the opposite. To investigate the mechanism of substrate binding, we analyzed crystal structures of an inactive mutant of the wheat glucosidase complexed with the natural substrate DIMBOA-Glc, wheat and rye glucosidases complexed with an aglycone DIMBOA, and wheat and rye glucosidases complexed with an inhibitor 2-fluoro-2-deoxy-beta-D-glucose. The binding position of substrate in the active site was determined but interaction between the substrate and Ser-464 or Leu-465 was not observed, although amino acid residues at these two positions are the only structural distinctions between wheat and rye glucosidase catalytic pockets. Variation at these two positions alters the width of the pocket entrance, which may relate to observed differences in substrate specificity. The side chain of Glu-462 that forms hydrogen bonds with the glucose moiety of DIMBOA-Glc moved deeper into the pocket upon substrate binding, and mutation of this residue dramatically decreased enzyme activity. | |||
Active-site architecture of benzoxazinone-glucoside beta-D-glucosidases in Triticeae.,Sue M, Nakamura C, Miyamoto T, Yajima S Plant Sci. 2011 Feb;180(2):268-75. Epub 2010 Sep 19. PMID:21421370<ref>PMID:21421370</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3aiu" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Beta-glucosidase|Beta-glucosidase]] | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Secale cereale]] | [[Category: Secale cereale]] | ||
[[Category: Miyamoto | [[Category: Miyamoto T]] | ||
[[Category: Nakamura | [[Category: Nakamura C]] | ||
[[Category: Sue | [[Category: Sue M]] | ||
[[Category: Yajima | [[Category: Yajima S]] | ||
Latest revision as of 18:47, 4 October 2023
Crystal structure of beta-glucosidase in ryeCrystal structure of beta-glucosidase in rye
Structural highlights
FunctionHGGL_SECCE Involved in defense of young plant parts against pests via the production of benzoxazolinones (hydroxamic acids) from hydroxamic acid glucosides. The preferred substrate is DIBOA-beta-D-glucoside. Can also use esculin and genistein glucoside as substrates, but no activity with salicin, p-nitrophenyl-alpha-glucoside or substrates related to cell wall components.[1] [PDB:3AIU] Publication Abstract from PubMedThe beta-D-glucosidases from wheat (Triticum aestivum) and rye (Secale cereale) hydrolyze benzoxazinone-glucose conjugates. Although wheat and rye glucosidases have high sequence identity, they have different substrate preferences; the wheat enzyme favors DIMBOA-Glc (2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one) over DIBOA-Glc (7-demethoxy-DIMBOA-Glc), whereas the rye enzyme preference is the opposite. To investigate the mechanism of substrate binding, we analyzed crystal structures of an inactive mutant of the wheat glucosidase complexed with the natural substrate DIMBOA-Glc, wheat and rye glucosidases complexed with an aglycone DIMBOA, and wheat and rye glucosidases complexed with an inhibitor 2-fluoro-2-deoxy-beta-D-glucose. The binding position of substrate in the active site was determined but interaction between the substrate and Ser-464 or Leu-465 was not observed, although amino acid residues at these two positions are the only structural distinctions between wheat and rye glucosidase catalytic pockets. Variation at these two positions alters the width of the pocket entrance, which may relate to observed differences in substrate specificity. The side chain of Glu-462 that forms hydrogen bonds with the glucose moiety of DIMBOA-Glc moved deeper into the pocket upon substrate binding, and mutation of this residue dramatically decreased enzyme activity. Active-site architecture of benzoxazinone-glucoside beta-D-glucosidases in Triticeae.,Sue M, Nakamura C, Miyamoto T, Yajima S Plant Sci. 2011 Feb;180(2):268-75. Epub 2010 Sep 19. PMID:21421370[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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