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1v08
From Proteopedia
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| - | == | + | |
| - | <StructureSection load='1v08' size='340' side='right' caption='[[1v08]], [[Resolution|resolution]] 1.90Å' scene=''> | + | ==Crystal structure of the Zea maze beta-glucosidase-1 in complex with gluco-tetrazole== |
| + | <StructureSection load='1v08' size='340' side='right'caption='[[1v08]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1v08]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1v08]] 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=1V08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V08 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NTZ:NOJIRIMYCINE+TETRAZOLE'>NTZ</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=1v08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v08 OCA], [https://pdbe.org/1v08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v08 RCSB], [https://www.ebi.ac.uk/pdbsum/1v08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v08 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [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> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/1v08_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/1v08_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=1v08 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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==See Also== | ==See Also== | ||
| - | *[[Beta-glucosidase|Beta-glucosidase]] | + | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Zea mays]] |
| - | [[Category: Bevan | + | [[Category: Bevan DR]] |
| - | [[Category: Czjzek | + | [[Category: Czjzek M]] |
| - | [[Category: Esen | + | [[Category: Esen A]] |
| - | [[Category: Henrissat | + | [[Category: Henrissat B]] |
| - | [[Category: Moriniere | + | [[Category: Moriniere J]] |
| - | [[Category: Verdoucq | + | [[Category: Verdoucq L]] |
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Current revision
Crystal structure of the Zea maze beta-glucosidase-1 in complex with gluco-tetrazole
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Categories: Large Structures | Zea mays | Bevan DR | Czjzek M | Esen A | Henrissat B | Moriniere J | Verdoucq L

