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New page: left|200px<br /><applet load="1ghr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ghr, resolution 2.2Å" /> '''THE THREE-DIMENSIONAL...
 
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[[Image:1ghr.gif|left|200px]]<br /><applet load="1ghr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ghr, resolution 2.2&Aring;" />
'''THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE SPECIFICITIES'''<br />


==Overview==
==THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE SPECIFICITIES==
The three-dimensional structures of (1--&gt;3)-beta-glucanase (EC 3.2.1.39), isoenzyme GII and (1--&gt;3,1--&gt;4)-beta-glucanase (EC 3.2.1.73) isoenzyme EII, from barley have been determined by x-ray crystallography at 2.2- to 2.3-A, resolution. The two classes of polysaccharide endohydrolase differ in, their substrate specificity and function. Thus, the, (1--&gt;3)-beta-glucanases, which are classified amongst the plant, "pathogenesis-related proteins," can hydrolyze (1--&gt;3)- and, (1--&gt;3,1--&gt;6)-beta-glucans of fungal cell walls and may therefore, contribute to plant defense strategies, while the, (1--&gt;3,1--&gt;4)-beta-glucanases function in plant cell wall hydrolysis, during mobilization of the endosperm in germinating grain or during the, growth of vegetative tissues. Both enzymes are alpha/beta-barrel, structures. The catalytic amino acid residues are located within deep, grooves which extend across the enzymes and which probably bind the, substrates. Because the polypeptide backbones of the two enzymes are, structurally very similar, the differences in their substrate, specificities, and hence their widely divergent functions, have been, acquired primarily by amino acid substitutions within the groove.
<StructureSection load='1ghr' size='340' side='right'caption='[[1ghr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ghr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHR FirstGlance]. <br>
</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ghr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghr OCA], [https://pdbe.org/1ghr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ghr RCSB], [https://www.ebi.ac.uk/pdbsum/1ghr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ghr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUB2_HORVU GUB2_HORVU] Functions in plant cell wall hydrolysis during mobilization of the endosperm in germinating grain or during the growth of vegetative tissues.
== 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/gh/1ghr_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=1ghr ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1GHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Active as [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GHR OCA].
*[[Glucanase 3D structures|Glucanase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities., Varghese JN, Garrett TP, Colman PM, Chen L, Hoj PB, Fincher GB, Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2785-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8146192 8146192]
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
[[Category: Licheninase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Garrett TPJ]]
[[Category: Garrett, T.P.J.]]
[[Category: Varghese JN]]
[[Category: Varghese, J.N.]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:04:15 2007''

Latest revision as of 07:25, 7 February 2024

THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE SPECIFICITIES

1ghr, resolution 2.20Å

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