1enx

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(New page: 200px<br /><applet load="1enx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1enx, resolution 1.5&Aring;" /> '''STRUCTURAL COMPARISON...)
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[[Image:1enx.gif|left|200px]]<br /><applet load="1enx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1enx, resolution 1.5&Aring;" />
 
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'''STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM TRICHODREMA REESEI'''<br />
 
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==Overview==
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==STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM TRICHODREMA REESEI==
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Three-dimensional structures of two major endo-1,4-xylanases, XYNI and, XYNII from Trichoderma reesei, have been determined by X-ray, crystallography. The amino acid sequences of both enzymes are highly, homologous (identity approximately 50%), and both XYNI and XYNII exist as, a single domain that contains two mostly antiparallel beta-sheets which, are packed against each other. The beta-sheet structure is twisted, forming a cleft where the active site is situated. Two glutamic acids in, the cleft, Glu75 and Glu164 in XYNI as well as Glu86 and Glu177 in XYNII, are most likely involved in catalysis. Inspection of the structures, reveals that the width of the active site cleft and the number of subsites, are different in XYNI and XYNII. The active site is narrower in XYNI and, probably contains only three subsites, whereas the number of subsites in, XYNII is most likely five. Variations in the surroundings of catalytic, residue Glu164XYNI/Glu177XYNII are thought to explain the pH optimum, differences observed in XYNI and XYNII.
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<StructureSection load='1enx' size='340' side='right'caption='[[1enx]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1enx]] 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=1ENX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ENX FirstGlance]. <br>
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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]] 1.5&#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=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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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=1enx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1enx OCA], [https://pdbe.org/1enx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1enx RCSB], [https://www.ebi.ac.uk/pdbsum/1enx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1enx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYN2_HYPJR XYN2_HYPJR] Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose (PubMed:1369024, Ref.5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747).<ref>PMID:1369024</ref> <ref>PMID:19556747</ref> <ref>PMID:7988708</ref> <ref>PMID:1369024</ref>
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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/en/1enx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1enx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Three-dimensional structures of two major endo-1,4-xylanases, XYNI and XYNII from Trichoderma reesei, have been determined by X-ray crystallography. The amino acid sequences of both enzymes are highly homologous (identity approximately 50%), and both XYNI and XYNII exist as a single domain that contains two mostly antiparallel beta-sheets which are packed against each other. The beta-sheet structure is twisted, forming a cleft where the active site is situated. Two glutamic acids in the cleft, Glu75 and Glu164 in XYNI as well as Glu86 and Glu177 in XYNII, are most likely involved in catalysis. Inspection of the structures reveals that the width of the active site cleft and the number of subsites are different in XYNI and XYNII. The active site is narrower in XYNI and probably contains only three subsites, whereas the number of subsites in XYNII is most likely five. Variations in the surroundings of catalytic residue Glu164XYNI/Glu177XYNII are thought to explain the pH optimum differences observed in XYNI and XYNII.
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==About this Structure==
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Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei.,Torronen A, Rouvinen J Biochemistry. 1995 Jan 24;34(3):847-56. PMID:7827044<ref>PMID:7827044</ref>
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1ENX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Active as [http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ENX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural comparison of two major endo-1,4-xylanases from Trichoderma reesei., Torronen A, Rouvinen J, Biochemistry. 1995 Jan 24;34(3):847-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7827044 7827044]
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</div>
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[[Category: Endo-1,4-beta-xylanase]]
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<div class="pdbe-citations 1enx" style="background-color:#fffaf0;"></div>
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[[Category: Hypocrea jecorina]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Rouvinen, J.]]
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__TOC__
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[[Category: Torronen, A.]]
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</StructureSection>
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[[Category: xylanase]]
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[[Category: Large Structures]]
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[[Category: Trichoderma reesei]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:09:48 2007''
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[[Category: Rouvinen J]]
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[[Category: Torronen A]]

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STRUCTURAL COMPARISON OF TWO MAJOR ENDO-1,4-BETA-XYLANASES FROM TRICHODREMA REESEI

PDB ID 1enx

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