1ghr

<StructureSection load='1ghr' size='340' side='right' caption='[[1ghr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ghr]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GHR FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<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=1ghr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ghr RCSB], [http://www.ebi.ac.uk/pdbsum/1ghr PDBsum]</span></td></tr>

[[http://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.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gh/1ghr_consurf.spt"</scriptWhenChecked>

</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].

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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:8146192<ref>PMID:8146192</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

*[[Glucanase|Glucanase]]

[[Category: Licheninase]]

[[Category: Garrett, T P.J]]

[[Category: Varghese, J N]]

[[Category: Hydrolase]]