1ghs

<table><tr><td colspan='2'>[[1ghs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GHS FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucan_endo-1,3-beta-D-glucosidase Glucan endo-1,3-beta-D-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.39 3.2.1.39] </span></td></tr>

[[https://www.uniprot.org/uniprot/E13B_HORVU E13B_HORVU]] May provide a degree of protection against microbial invasion of germinated barley grain through its ability to degrade fungal cell wall polysaccharides.

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== 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>

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== References ==

<references/>

[[Category: Glucan endo-1,3-beta-D-glucosidase]]

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

[[Category: Varghese, J N]]

[[Category: Hydrolase]]