3lgr

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[[Image:3lgr.jpg|left|200px]]
 
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==Xylanase II from Trichoderma reesei cocrystallized with tris-dipicolinate europium==
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The line below this paragraph, containing "STRUCTURE_3lgr", creates the "Structure Box" on the page.
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<StructureSection load='3lgr' size='340' side='right'caption='[[3lgr]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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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'>[[3lgr]] 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=3LGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LGR 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]] 1.64&#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=EU:EUROPIUM+ION'>EU</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PDC:PYRIDINE-2,6-DICARBOXYLIC+ACID'>PDC</scene></td></tr>
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{{STRUCTURE_3lgr| PDB=3lgr | 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=3lgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgr OCA], [https://pdbe.org/3lgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lgr RCSB], [https://www.ebi.ac.uk/pdbsum/3lgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lgr 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tris-dipicolinate lanthanide complexes were used to prepare derivative crystals of six proteins: hen egg-white lysozyme, turkey egg-white lysozyme, thaumatin from Thaumatococcus daniellii, urate oxidase from Aspergillus flavus, porcine pancreatic elastase and xylanase from Trichoderma reesei. Diffraction data were collected using either synchrotron radiation or X-rays from a laboratory source. In all cases, the complex turned out to be bound to the protein and the phases determined using the anomalous scattering of the lanthanide led to high-quality electron-density maps. The binding mode of the complex was characterized from the refined structures. The lanthanide tris-dipicolinate was found to bind through interactions between carboxylate groups of the dipicolinate ligands and hydrogen-bond donor groups of the protein. In each binding site, one enantiomeric form of the complex is selected from the racemic solution according to the specific site topology. For hen egg-white lysozyme and xylanase, derivative crystals obtained by cocrystallization belonged to a new monoclinic C2 crystal form that diffracted to high resolution.
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===Xylanase II from Trichoderma reesei cocrystallized with tris-dipicolinate europium===
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A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction.,Pompidor G, Maury O, Vicat J, Kahn R Acta Crystallogr D Biol Crystallogr. 2010 Jul;66(Pt 7):762-9. Epub 2010, Jun 19. PMID:20606256<ref>PMID:20606256</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_20606256}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3lgr" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20606256 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20606256}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3lgr]] is a 1 chain structure with 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=3LGR OCA].
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[[Category: Trichoderma reesei]]
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[[Category: Kahn R]]
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==Reference==
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[[Category: Maury O]]
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<ref group="xtra">PMID:20606256</ref><references group="xtra"/>
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[[Category: Pompidor G]]
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Hypocrea jecorina]]
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[[Category: Kahn, R.]]
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[[Category: Maury, O.]]
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[[Category: Pompidor, G.]]
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Current revision

Xylanase II from Trichoderma reesei cocrystallized with tris-dipicolinate europium

PDB ID 3lgr

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