2cyg

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(New page: 200px<br /><applet load="2cyg" size="350" color="white" frame="true" align="right" spinBox="true" caption="2cyg, resolution 1.45&Aring;" /> '''Crystal structure at...)
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==Overview==
==Overview==
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Resolution of the crystal structure of the banana fruit, endo-beta-1,3-glucanase by synchrotron X-ray diffraction at 1.45-A, resolution revealed that the enzyme possesses the eightfold beta/alpha, architecture typical for family 17 glycoside hydrolases. 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 beta-1,3 linked glucan, trisaccharide as a substrate confirmed that the enzyme readily, accommodates a beta-1,3-glycosidic linkage in the slightly curved, catalytic groove between the glucose units in positions -2 and -1 because, of the particular orientation of residue Tyr33 delimiting subsite -2. The, location of Phe177 in the proximity of subsite +1 suggested that the, banana glucanase might also cleave beta-1,6-branched glucans. Enzymatic, assays using pustulan as a substrate demonstrated that the banana, glucanase can also cleave beta-1,6-glucans as was predicted from docking, experiments. Similar to many other plant endo-beta-1,3-glucanases, the, banana glucanase exhibits allergenic properties because of the occurrence, of well-conserved IgE-binding epitopes on the surface of the enzyme. These, epitopes might trigger some cross-reactions toward IgE antibodies and thus, account for the IgE-binding cross-reactivity frequently reported in, patients with the latex-fruit syndrome.
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Resolution of the crystal structure of the banana fruit endo-beta-1,3-glucanase by synchrotron X-ray diffraction at 1.45-A resolution revealed that the enzyme possesses the eightfold beta/alpha architecture typical for family 17 glycoside hydrolases. 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 beta-1,3 linked glucan trisaccharide as a substrate confirmed that the enzyme readily accommodates a beta-1,3-glycosidic linkage in the slightly curved catalytic groove between the glucose units in positions -2 and -1 because of the particular orientation of residue Tyr33 delimiting subsite -2. The location of Phe177 in the proximity of subsite +1 suggested that the banana glucanase might also cleave beta-1,6-branched glucans. Enzymatic assays using pustulan as a substrate demonstrated that the banana glucanase can also cleave beta-1,6-glucans as was predicted from docking experiments. Similar to many other plant endo-beta-1,3-glucanases, the banana glucanase exhibits allergenic properties because of the occurrence of well-conserved IgE-binding epitopes on the surface of the enzyme. These epitopes might trigger some cross-reactions toward IgE antibodies and thus account for the IgE-binding cross-reactivity frequently reported in patients with the latex-fruit syndrome.
==About this Structure==
==About this Structure==
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[[Category: Barre, A.]]
[[Category: Barre, A.]]
[[Category: Czjzek, M.]]
[[Category: Czjzek, M.]]
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[[Category: Damme, E.J.M.Van.]]
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[[Category: Damme, E J.M Van.]]
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[[Category: Peumans, W.J.]]
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[[Category: Peumans, W J.]]
[[Category: Receveur-Brechot, V.]]
[[Category: Receveur-Brechot, V.]]
[[Category: Rouge, P.]]
[[Category: Rouge, P.]]
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[[Category: endo-beta-1]]
[[Category: endo-beta-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:51:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:53:42 2008''

Revision as of 14:53, 21 February 2008


2cyg, resolution 1.45Å

Drag the structure with the mouse to rotate

Crystal structure at 1.45- resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome

Overview

Resolution of the crystal structure of the banana fruit endo-beta-1,3-glucanase by synchrotron X-ray diffraction at 1.45-A resolution revealed that the enzyme possesses the eightfold beta/alpha architecture typical for family 17 glycoside hydrolases. 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 beta-1,3 linked glucan trisaccharide as a substrate confirmed that the enzyme readily accommodates a beta-1,3-glycosidic linkage in the slightly curved catalytic groove between the glucose units in positions -2 and -1 because of the particular orientation of residue Tyr33 delimiting subsite -2. The location of Phe177 in the proximity of subsite +1 suggested that the banana glucanase might also cleave beta-1,6-branched glucans. Enzymatic assays using pustulan as a substrate demonstrated that the banana glucanase can also cleave beta-1,6-glucans as was predicted from docking experiments. Similar to many other plant endo-beta-1,3-glucanases, the banana glucanase exhibits allergenic properties because of the occurrence of well-conserved IgE-binding epitopes on the surface of the enzyme. These epitopes might trigger some cross-reactions toward IgE antibodies and thus account for the IgE-binding cross-reactivity frequently reported in patients with the latex-fruit syndrome.

About this Structure

2CYG is a Single protein structure of sequence from Musa acuminata. Active as Glucan endo-1,3-beta-D-glucosidase, with EC number 3.2.1.39 Full crystallographic information is available from OCA.

Reference

Crystal structure at 1.45-A resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome., Receveur-Brechot V, Czjzek M, Barre A, Roussel A, Peumans WJ, Van Damme EJ, Rouge P, Proteins. 2006 Apr 1;63(1):235-42. PMID:16421930

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