1h49

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[[Image:1h49.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE==
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The line below this paragraph, containing "STRUCTURE_1h49", creates the "Structure Box" on the page.
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<StructureSection load='1h49' size='340' side='right'caption='[[1h49]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1h49]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H49 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<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=HBO:2,4-DIHYDROXY-7-(METHYLOXY)-2H-1,4-BENZOXAZIN-3(4H)-ONE'>HBO</scene></td></tr>
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{{STRUCTURE_1h49| PDB=1h49 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h49 OCA], [https://pdbe.org/1h49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h49 RCSB], [https://www.ebi.ac.uk/pdbsum/1h49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h49 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HGGL1_MAIZE HGGL1_MAIZE] Is implicated in many functions such as ABA metabolism, hydrolysis of conjugated gibberellins, conversion of storage forms of cytokinins to active forms. Also acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth. The preferred substrate is DIMBOA-beta-D-glucoside. Hydrolyzes the chromogenic substrate 6-bromo-2-naphthyl-beta-D-glucoside (6BNGlc) and various artificial aryl beta-glucosides. No activity with cellobiose, arbutin, gentiobiose, linamarin or dhurrin as substrates.<ref>PMID:10099619</ref> <ref>PMID:16668611</ref> <ref>PMID:10099619</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h4/1h49_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h49 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Plant beta-glucosidases display varying substrate specificities. The maize beta-glucosidase isozyme Glu1 (ZmGlu1) hydrolyzes a broad spectrum of substrates in addition to its natural substrate DIMBOA-Glc (2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxaxin-3-one), whereas the sorghum beta-glucosidase isozyme Dhr1 (SbDhr1) hydrolyzes exclusively its natural substrate dhurrin (p-hydroxy-(S)-mandelonitrile-beta-d-glucoside). Structural data from cocrystals of enzyme-substrate and enzyme-aglycone complexes have shown that five amino acid residues (Phe198, Phe205, Trp378, Phe466, and Ala467) are located in the aglycone-binding site of ZmGlu1 and form the basis of aglycone recognition and binding, hence substrate specificity. To study the mechanism of substrate specificity further, mutant beta-glucosidases were generated by replacing Phe198, Phe205, Asp261, Met263, Phe377, Phe466, Ala467, and Phe473 of Glu1 by Dhr1 counterparts. The effects of mutations on enzyme activity and substrate specificity were studied using both natural and artificial substrates. The simple mutant replacing Phe198 by a valine had the most drastic effect on activity, because the capacity of this enzyme to hydrolyze beta-glucosides was almost completely abolished. The analysis of this mutation was completed by a structural study of the double mutant ZmGlu1-E191D,F198V in complex with the natural substrate. The structure reveals that the single mutation F198V causes a cascade of conformational changes, which are unpredictable by standard molecular modeling techniques. Some other mutations led to drastic effects: replacing Asp261 by an asparagine decreases the catalytic efficiency of this simple mutant by 75% although replacing Tyr473 by a phenylalanine increase its efficiency by 300% and also provides a new substrate specificity by hydrolyzing dhurrin.
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===CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE===
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Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases.,Verdoucq L, Czjzek M, Moriniere J, Bevan DR, Esen A J Biol Chem. 2003 Jul 4;278(27):25055-62. Epub 2003 Apr 8. PMID:12684498<ref>PMID:12684498</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1h49" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12684498 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12684498}}
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==About this Structure==
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[[1h49]] is a 2 chain structure of [[Beta-glucosidase]] with sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H49 OCA].
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==See Also==
==See Also==
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*[[Beta-glucosidase]]
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*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:012684498</ref><ref group="xtra">PMID:011106394</ref><references group="xtra"/>
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__TOC__
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[[Category: Beta-glucosidase]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Zea mays]]
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[[Category: Bevan, D R.]]
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[[Category: Bevan DR]]
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[[Category: Czjzek, M.]]
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[[Category: Czjzek M]]
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[[Category: Esen, A.]]
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[[Category: Esen A]]
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[[Category: Henrissat, B.]]
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[[Category: Henrissat B]]
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[[Category: Moriniere, J.]]
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[[Category: Moriniere J]]
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[[Category: Verdoucq, L.]]
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[[Category: Verdoucq L]]
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[[Category: Beta-glucosidase]]
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[[Category: Family 1]]
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[[Category: Glycoside hydrolase]]
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[[Category: Hydrolase]]
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[[Category: Inactive mutant e191d]]
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[[Category: Retention of the anomeric configuration]]
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Current revision

CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE

PDB ID 1h49

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