1e4l

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(New page: 200px<br /><applet load="1e4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e4l, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1e4l.gif|left|200px]]<br /><applet load="1e4l" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e4l, resolution 2.2&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZM GLU191ASP'''<br />
 
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==Overview==
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==Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZM Glu191Asp==
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The mechanism and the site of substrate (i.e., aglycone) recognition and, specificity were investigated in maize beta-glucosidase (Glu1) by x-ray, crystallography by using crystals of a catalytically inactive mutant, (Glu1E191D) in complex with the natural substrate, 2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one, (DIMBOAGlc), the free aglycone DIMBOA, and competitive inhibitor, para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin). The structures of, these complexes and of the free enzyme were solved at 2.1-, 2.1-, 2.0-, and 2.2-A resolution, respectively. The structural data from the complexes, allowed us to visualize an intact substrate, free aglycone, or a, competitive inhibitor in the slot-like active site of a beta-glucosidase., These data show that the aglycone moiety of the substrate is sandwiched, between W378 on one side and F198, F205, and F466 on the other. Thus, specific conformations of these four hydrophobic amino acids and the shape, of the aglycone-binding site they form determine aglycone recognition and, substrate specificity in Glu1. In addition to these four residues, A467, interacts with the 7-methoxy group of DIMBOA. All residues but W378 are, variable among beta-glucosidases that differ in substrate specificity, supporting the conclusion that these sites are the basis of aglycone, recognition and binding (i.e., substrate specificity) in, beta-glucosidases. The data also provide a plausible explanation for the, competitive binding of dhurrin to maize beta-glucosidases with high, affinity without being hydrolyzed.
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<StructureSection load='1e4l' size='340' side='right'caption='[[1e4l]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e4l]] 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=1E4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E4L 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]] 2.2&#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=GOL:GLYCEROL'>GOL</scene></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=1e4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e4l OCA], [https://pdbe.org/1e4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e4l RCSB], [https://www.ebi.ac.uk/pdbsum/1e4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e4l 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/e4/1e4l_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=1e4l 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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The mechanism and the site of substrate (i.e., aglycone) recognition and specificity were investigated in maize beta-glucosidase (Glu1) by x-ray crystallography by using crystals of a catalytically inactive mutant (Glu1E191D) in complex with the natural substrate 2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOAGlc), the free aglycone DIMBOA, and competitive inhibitor para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin). The structures of these complexes and of the free enzyme were solved at 2.1-, 2.1-, 2.0-, and 2.2-A resolution, respectively. The structural data from the complexes allowed us to visualize an intact substrate, free aglycone, or a competitive inhibitor in the slot-like active site of a beta-glucosidase. These data show that the aglycone moiety of the substrate is sandwiched between W378 on one side and F198, F205, and F466 on the other. Thus, specific conformations of these four hydrophobic amino acids and the shape of the aglycone-binding site they form determine aglycone recognition and substrate specificity in Glu1. In addition to these four residues, A467 interacts with the 7-methoxy group of DIMBOA. All residues but W378 are variable among beta-glucosidases that differ in substrate specificity, supporting the conclusion that these sites are the basis of aglycone recognition and binding (i.e., substrate specificity) in beta-glucosidases. The data also provide a plausible explanation for the competitive binding of dhurrin to maize beta-glucosidases with high affinity without being hydrolyzed.
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==About this Structure==
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The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes.,Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13555-60. PMID:11106394<ref>PMID:11106394</ref>
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1E4L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E4L OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes., Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13555-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106394 11106394]
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</div>
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[[Category: Beta-glucosidase]]
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<div class="pdbe-citations 1e4l" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Zea mays]]
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[[Category: Bevan, D.R.]]
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[[Category: Cicek, M.]]
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[[Category: Czjzek, M.]]
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[[Category: Esen, A.]]
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[[Category: Henrissat, B.]]
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[[Category: GOL]]
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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: inactive mutant e191d]]
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[[Category: retention of the anomeric configuration]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:46:27 2007''
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==See Also==
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*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Zea mays]]
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[[Category: Bevan DR]]
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[[Category: Cicek M]]
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[[Category: Czjzek M]]
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[[Category: Esen A]]
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[[Category: Henrissat B]]

Current revision

Crystal structure of the inactive mutant Monocot (Maize ZMGlu1) beta-glucosidase ZM Glu191Asp

PDB ID 1e4l

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