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[[Image:1e1f.png|left|200px]]


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==Crystal structure of a Monocot (Maize ZMGlu1) beta-glucosidase in complex with p-Nitrophenyl-beta-D-thioglucoside==
The line below this paragraph, containing "STRUCTURE_1e1f", creates the "Structure Box" on the page.
<StructureSection load='1e1f' size='340' side='right'caption='[[1e1f]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1e1f]] 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=1E1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E1F FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=PSG:PARA-NITROPHENYL+1-THIO-BETA-D-GLUCOPYRANOSIDE'>PSG</scene></td></tr>
{{STRUCTURE_1e1f|  PDB=1e1f  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e1f OCA], [https://pdbe.org/1e1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e1f RCSB], [https://www.ebi.ac.uk/pdbsum/1e1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e1f ProSAT]</span></td></tr>
</table>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e1/1e1f_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1e1f ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The maize beta-glucosidase isoenzymes ZMGlu1 and ZMGlu2 hydrolyse the abundant natural substrate DIMBOAGlc (2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one), whose aglycone DIMBOA (2,4-hydroxy-7-methoxy-1,4-benzoxazin-3-one) is the major defence chemical protecting seedlings and young plant parts against herbivores and other pests. The two isoenzymes hydrolyse DIMBOAGlc with similar kinetics but differ from each other and their sorghum homologues with respect to specificity towards other substrates. To gain insights into the mechanism of substrate (i.e. aglycone) specificity between the two maize isoenzymes and their sorghum homologues, ZMGlu1 was produced in Escherichia coli, purified, crystallized and its structure solved at 2.5 Angstrom resolution by X-ray crystallography. In addition, the complex of ZMGlu1 with the non-hydrolysable inhibitor p-nitrophenyl beta-D-thioglucoside was crystallized and, based on the partial electron density, a model for the inhibitor molecule within the active site is proposed. The inhibitor is located in a slot-like active site where its aromatic aglycone is held by stacking interactions with Trp-378. Whereas some of the atoms on the non-reducing end of the glucose moiety can be modelled on the basis of the electron density, most of the inhibitor atoms are highly disordered. This is attributed to the requirement of the enzyme to accommodate two different species, namely the substrate in its ground state and in its distorted conformation, for catalysis.


===CRYSTAL STRUCTURE OF A MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE IN COMPLEX WITH P-NITROPHENYL-BETA-D-THIOGLUCOSIDE===
Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside.,Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, Esen A Biochem J. 2001 Feb 15;354(Pt 1):37-46. PMID:11171077<ref>PMID:11171077</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1e1f" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_11171077}}, adds the Publication Abstract to the page
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 11171077 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_11171077}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1E1F is a 2 chains structure of sequences 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=1E1F OCA].
 
==Reference==
<ref group="xtra">PMID:11171077</ref><references group="xtra"/>
[[Category: Beta-glucosidase]]
[[Category: Zea mays]]
[[Category: Zea mays]]
[[Category: Bevan, D R.]]
[[Category: Bevan DR]]
[[Category: Cicek, M.]]
[[Category: Cicek M]]
[[Category: Czjzek, M.]]
[[Category: Czjzek M]]
[[Category: Esen, A.]]
[[Category: Esen A]]
[[Category: Henrissat, B.]]
[[Category: Henrissat B]]
[[Category: Beta-glucosidase]]
[[Category: Family 1]]
[[Category: Glycoside hydrolase]]
[[Category: Pnp-beta-d-thioglucoside]]
[[Category: Retention of the anomeric configuration]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:51:33 2009''

Latest revision as of 11:10, 6 December 2023

Crystal structure of a Monocot (Maize ZMGlu1) beta-glucosidase in complex with p-Nitrophenyl-beta-D-thioglucosideCrystal structure of a Monocot (Maize ZMGlu1) beta-glucosidase in complex with p-Nitrophenyl-beta-D-thioglucoside

Structural highlights

1e1f is a 2 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The maize beta-glucosidase isoenzymes ZMGlu1 and ZMGlu2 hydrolyse the abundant natural substrate DIMBOAGlc (2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one), whose aglycone DIMBOA (2,4-hydroxy-7-methoxy-1,4-benzoxazin-3-one) is the major defence chemical protecting seedlings and young plant parts against herbivores and other pests. The two isoenzymes hydrolyse DIMBOAGlc with similar kinetics but differ from each other and their sorghum homologues with respect to specificity towards other substrates. To gain insights into the mechanism of substrate (i.e. aglycone) specificity between the two maize isoenzymes and their sorghum homologues, ZMGlu1 was produced in Escherichia coli, purified, crystallized and its structure solved at 2.5 Angstrom resolution by X-ray crystallography. In addition, the complex of ZMGlu1 with the non-hydrolysable inhibitor p-nitrophenyl beta-D-thioglucoside was crystallized and, based on the partial electron density, a model for the inhibitor molecule within the active site is proposed. The inhibitor is located in a slot-like active site where its aromatic aglycone is held by stacking interactions with Trp-378. Whereas some of the atoms on the non-reducing end of the glucose moiety can be modelled on the basis of the electron density, most of the inhibitor atoms are highly disordered. This is attributed to the requirement of the enzyme to accommodate two different species, namely the substrate in its ground state and in its distorted conformation, for catalysis.

Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside.,Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, Esen A Biochem J. 2001 Feb 15;354(Pt 1):37-46. PMID:11171077[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Cicek M, Esen A. Expression of soluble and catalytically active plant (monocot) beta-glucosidases in E. coli. Biotechnol Bioeng. 1999 May 20;63(4):392-400. PMID:10099619
  2. Esen A. Purification and Partial Characterization of Maize (Zea mays L.) beta-Glucosidase. Plant Physiol. 1992 Jan;98(1):174-82. PMID:16668611
  3. Cicek M, Esen A. Expression of soluble and catalytically active plant (monocot) beta-glucosidases in E. coli. Biotechnol Bioeng. 1999 May 20;63(4):392-400. PMID:10099619
  4. Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, Esen A. Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside. Biochem J. 2001 Feb 15;354(Pt 1):37-46. PMID:11171077

1e1f, resolution 2.60Å

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