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The electronegatively charged catalytic central cleft harbors the two glutamate residues (Glu94 and Glu236) acting as hydrogen donor and nucleophile residue, respectively. Modeling using a \u03b2\u20101,3 linked glucan trisaccharide as a substrate confirmed that the enzyme readily accommodates a \u03b2\u20101,3\u2010glycosidic linkage in the slightly curved catalytic groove between the glucose units in positions \u22122 and \u22121 because of the particular orientation of residue Tyr33 delimiting subsite \u22122. The location of Phe177 in the proximity of subsite +1 suggested that the banana glucanase might also cleave \u03b2\u20101,6\u2010branched glucans. Enzymatic assays using pustulan as a substrate demonstrated that the banana glucanase can also cleave \u03b2\u20101,6\u2010glucans as was predicted from docking experiments. Similar to many other plant endo\u2010\u03b2\u20101,3\u2010glucanases, the banana glucanase exhibits allergenic properties because of the occurrence of well\u2010conserved IgE\u2010binding epitopes on the surface of the enzyme. These epitopes might trigger some cross\u2010reactions toward IgE antibodies and thus account for the IgE\u2010binding cross\u2010reactivity frequently reported in patients with the latex\u2010fruit syndrome. Proteins 2006. \u00a9 2006 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.20876","type":"journal-article","created":{"date-parts":[[2006,1,18]],"date-time":"2006-01-18T23:46:42Z","timestamp":1137628002000},"page":"235-242","source":"Crossref","is-referenced-by-count":41,"title":["Crystal structure at 1.45\u2010\u00c5 resolution of the major allergen endo\u2010\u03b2\u20101,3\u2010glucanase of banana as a molecular basis for the latex\u2010fruit syndrome"],"prefix":"10.1002","volume":"63","author":[{"given":"V\u00e9ronique","family":"Receveur\u2010Br\u00e9chot","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mirjam","family":"Czjzek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annick","family":"Barre","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alain","family":"Roussel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Willy J.","family":"Peumans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Els J.M.","family":"Van Damme","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierre","family":"Roug\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,1,18]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/BST0300901"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1042\/BST0300935"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0091-6749(95)70004-8"},{"key":"e_1_2_6_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2222.1996.tb00101.x"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1042\/BST0300930"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.67.7.2883-2894.2001"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2222.1995.tb01114.x"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2222.2002.01312.x"},{"key":"e_1_2_6_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0091-6749(98)70251-9"},{"key":"e_1_2_6_11_2","unstructured":"BeezholdDH ReschkeGL HickeyVL.Hevea brasiliensislipid transfer precursor protein mRNA partial cs. 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