1h49

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==CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE==
==CRYSTAL STRUCTURE OF THE INACTIVE DOUBLE MUTANT OF THE MAIZE BETA-GLUCOSIDASE ZMGLU1-E191D-F198V IN COMPLEX WITH DIMBOA-GLUCOSIDE==
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<StructureSection load='1h49' size='340' side='right' caption='[[1h49]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='1h49' size='340' side='right'caption='[[1h49]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1h49]] is a 2 chain structure 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H49 FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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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</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e1e|1e1e]], [[1e1f|1e1f]], [[1e4l|1e4l]], [[1e4n|1e4n]], [[1e55|1e55]], [[1e56|1e56]], [[1hxj|1hxj]]</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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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></td></tr>
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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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<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=1h49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h49 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h49 RCSB], [http://www.ebi.ac.uk/pdbsum/1h49 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/BGLC_MAIZE BGLC_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:16668611</ref> <ref>PMID:11106394</ref> <ref>PMID:10099619</ref>
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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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h4/1h49_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 1h49" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Beta-glucosidase|Beta-glucosidase]]
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*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Beta-glucosidase]]
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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: 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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