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1eg1

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[[Image:1eg1.gif|left|200px]]
 
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==ENDOGLUCANASE I FROM TRICHODERMA REESEI==
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The line below this paragraph, containing "STRUCTURE_1eg1", creates the "Structure Box" on the page.
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<StructureSection load='1eg1' size='340' side='right'caption='[[1eg1]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1eg1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EG1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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{{STRUCTURE_1eg1| PDB=1eg1 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eg1 OCA], [https://pdbe.org/1eg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eg1 RCSB], [https://www.ebi.ac.uk/pdbsum/1eg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eg1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GUN1_HYPJE GUN1_HYPJE] The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1eg1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1eg1 ConSurf].
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<div style="clear:both"></div>
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'''ENDOGLUCANASE I FROM TRICHODERMA REESEI'''
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==See Also==
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Cellulose is the most abundant polymer in the biosphere. Although generally resistant to degradation, it may be hydrolysed by cellulolytic organisms that have evolved a variety of structurally distinct enzymes, cellobiohydrolases and endoglucanases, for this purpose. Endoglucanase I (EG I) is the major endoglucanase produced by the cellulolytic fungus Trichoderma reesei, accounting for 5 to 10% of the total amount of cellulases produced by this organism. Together with EG I from Humicola insolens and T. reesei cellobiohydrolase I (CBH I), the enzyme is classified into family 7 of the glycosyl hydrolases, and it catalyses hydrolysis with a net retention of the anomeric configuration.The structure of the catalytic core domain (residues 1 to 371) of EG I from T. reesei has been determined at 3.6 A resolution by the molecular replacement method using the structures of T. reesei CBH I and H. insolens EG I as search models. By employing the 2-fold non-crystallographic symmetry (NCS), the structure was refined successfully, despite the limited resolution. The final model has an R-factor of 0.201 (Rfree 0.258).The structure of EG I reveals an extended, open substrate-binding cleft, rather than a tunnel as found in the homologous cellobiohydrolase CBH I. This confirms the earlier proposal that the tunnel-forming loops in CBH I have been deleted in EG I, which has resulted in an open active site in EG I, enabling it to function as an endoglucanase. Comparison of the structure of EG I with several related enzymes reveals structural similarities, and differences that relate to their biological function in degrading particular substrates. A possible structural explanation of the drastically different pH profiles of T. reesei and H. insolens EG I is proposed.
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[[Category: Large Structures]]
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[[Category: Trichoderma reesei]]
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==About this Structure==
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[[Category: Jones TA]]
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1EG1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EG1 OCA].
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[[Category: Kleywegt GJ]]
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[[Category: Zou J-Y]]
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==Reference==
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The crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymes., Kleywegt GJ, Zou JY, Divne C, Davies GJ, Sinning I, Stahlberg J, Reinikainen T, Srisodsuk M, Teeri TT, Jones TA, J Mol Biol. 1997 Sep 26;272(3):383-97. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9325098 9325098]
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[[Category: Cellulase]]
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[[Category: Hypocrea jecorina]]
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[[Category: Single protein]]
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[[Category: Jones, T A.]]
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[[Category: Kleywegt, G J.]]
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[[Category: Zou, J Y.]]
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[[Category: Cellulose degradation]]
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[[Category: Endoglucanase]]
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[[Category: Mutation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:03:17 2008''
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Current revision

ENDOGLUCANASE I FROM TRICHODERMA REESEI

PDB ID 1eg1

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