2dfb

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[[Image:2dfb.png|left|200px]]
 
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{{STRUCTURE_2dfb| PDB=2dfb | SCENE= }}
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==Xylanase II from Tricoderma reesei at 100K==
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<StructureSection load='2dfb' size='340' side='right'caption='[[2dfb]], [[Resolution|resolution]] 1.11&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2dfb]] is a 1 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=2DFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DFB 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]] 1.11&#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=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2dfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dfb OCA], [https://pdbe.org/2dfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dfb RCSB], [https://www.ebi.ac.uk/pdbsum/2dfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dfb 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/df/2dfb_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=2dfb 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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An orthorhombic crystal of xylanase II from Trichoderma reesei was grown in the presence of sodium iodide. Crystal structures at atomic resolution were determined at 100 and 293 K. Protein molecules were aligned along a crystallographic twofold screw axis, forming a helically extended polymer-like chain mediated by an iodide ion. The iodide ion connected main-chain peptide groups between two adjacent molecules by an N-H...I-...H-N hydrogen-bond bridge, thus contributing to regulation of the molecular arrangement and suppression of the rigid-body motion in the crystal with high diffraction quality. The structure at 293 K showed considerable thermal motion in the loop regions connecting the beta-strands that form the active-site cleft. TLS model analysis of the thermal motion and a comparison between this structure and that at 100 K suggest that the fluctuation of these loop regions is attributable to the hinge-like movement of the beta-strands.
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===Xylanase II from Tricoderma reesei at 100K===
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Structure of an orthorhombic form of xylanase II from Trichoderma reesei and analysis of thermal displacement.,Watanabe N, Akiba T, Kanai R, Harata K Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):784-92. Epub 2006, Jun 20. PMID:16790934<ref>PMID:16790934</ref>
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{{ABSTRACT_PUBMED_16790934}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2dfb" style="background-color:#fffaf0;"></div>
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[[2dfb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DFB OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:016790934</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Large Structures]]
[[Category: Trichoderma reesei]]
[[Category: Trichoderma reesei]]
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[[Category: Akiba, T.]]
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[[Category: Akiba T]]
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[[Category: Harata, K.]]
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[[Category: Harata K]]
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[[Category: Bent beta sheet]]
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[[Category: Hydrolase]]
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Current revision

Xylanase II from Tricoderma reesei at 100K

PDB ID 2dfb

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