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| - | [[Image:2cyg.gif|left|200px]] | |
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| - | <!--
| + | ==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== |
| - | The line below this paragraph, containing "STRUCTURE_2cyg", creates the "Structure Box" on the page.
| + | <StructureSection load='2cyg' size='340' side='right'caption='[[2cyg]], [[Resolution|resolution]] 1.45Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[2cyg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Musa_acuminata Musa acuminata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CYG FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</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=2cyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cyg OCA], [https://pdbe.org/2cyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cyg RCSB], [https://www.ebi.ac.uk/pdbsum/2cyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cyg ProSAT]</span></td></tr> |
| - | {{STRUCTURE_2cyg| PDB=2cyg | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/E13C_MUSAC E13C_MUSAC] Possesses beta-1,3-endoglucanase activity in vitro (PubMed:10672030). May play a role in fruit pulp softening process (Probable). Can cleave beta-1,6-branched glucans in vitro (PubMed:16421930).<ref>PMID:10672030</ref> <ref>PMID:16421930</ref> <ref>PMID:10672030</ref> <ref>PMID:20467747</ref> |
| | + | == 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/cy/2cyg_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=2cyg ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | 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. |
| | | | |
| - | '''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'''
| + | 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<ref>PMID:16421930</ref> |
| - | | + | |
| - | | + | |
| - | ==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==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 2CYG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Musa_acuminata Musa acuminata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CYG OCA].
| + | </div> |
| | + | <div class="pdbe-citations 2cyg" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16421930 16421930]
| + | *[[Glucanase 3D structures|Glucanase 3D structures]] |
| - | [[Category: Glucan endo-1,3-beta-D-glucosidase]] | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Musa acuminata]] | | [[Category: Musa acuminata]] |
| - | [[Category: Single protein]]
| + | [[Category: Barre A]] |
| - | [[Category: Barre, A.]] | + | [[Category: Czjzek M]] |
| - | [[Category: Czjzek, M.]] | + | [[Category: Peumans WJ]] |
| - | [[Category: Damme, E J.M Van.]]
| + | [[Category: Receveur-Brechot V]] |
| - | [[Category: Peumans, W J.]] | + | [[Category: Rouge P]] |
| - | [[Category: Receveur-Brechot, V.]] | + | [[Category: Roussel A]] |
| - | [[Category: Rouge, P.]] | + | [[Category: Van Damme EJM]] |
| - | [[Category: Roussel, A.]] | + | |
| - | [[Category: Allergen]] | + | |
| - | [[Category: B-cell epitope]]
| + | |
| - | [[Category: Banana]]
| + | |
| - | [[Category: Endo-beta-1,3-glucanase]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:21:24 2008''
| + | |
| Structural highlights
Function
E13C_MUSAC Possesses beta-1,3-endoglucanase activity in vitro (PubMed:10672030). May play a role in fruit pulp softening process (Probable). Can cleave beta-1,6-branched glucans in vitro (PubMed:16421930).[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Peumans WJ, Barre A, Derycke V, Rougé P, Zhang W, May GD, Delcour JA, Van Leuven F, Van Damme EJ. Purification, characterization and structural analysis of an abundant beta-1,3-glucanase from banana fruit. Eur J Biochem. 2000 Feb;267(4):1188-95. PMID:10672030 doi:10.1046/j.1432-1327.2000.01117.x
- ↑ Receveur-Brechot V, Czjzek M, Barre A, Roussel A, Peumans WJ, Van Damme EJ, Rouge P. 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. Proteins. 2006 Apr 1;63(1):235-42. PMID:16421930 doi:http://dx.doi.org/10.1002/prot.20876
- ↑ Peumans WJ, Barre A, Derycke V, Rougé P, Zhang W, May GD, Delcour JA, Van Leuven F, Van Damme EJ. Purification, characterization and structural analysis of an abundant beta-1,3-glucanase from banana fruit. Eur J Biochem. 2000 Feb;267(4):1188-95. PMID:10672030 doi:10.1046/j.1432-1327.2000.01117.x
- ↑ Roy Choudhury S, Roy S, Singh SK, Sengupta DN. Molecular characterization and differential expression of beta-1,3-glucanase during ripening in banana fruit in response to ethylene, auxin, ABA, wounding, cold and light-dark cycles. Plant Cell Rep. 2010 Aug;29(8):813-28. PMID:20467747 doi:10.1007/s00299-010-0866-0
- ↑ Receveur-Brechot V, Czjzek M, Barre A, Roussel A, Peumans WJ, Van Damme EJ, Rouge P. 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. Proteins. 2006 Apr 1;63(1):235-42. PMID:16421930 doi:http://dx.doi.org/10.1002/prot.20876
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