5tc9: Difference between revisions

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-'''Unreleased structure'''
-The entry 5tc9 is ON HOLD
+==Wild type TrCel7A catalytic domain in a closed state==
+<StructureSection load='5tc9' size='340' side='right'caption='[[5tc9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5tc9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei_QM6a Trichoderma reesei QM6a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TC9 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GD3:GADOLINIUM+ION'>GD3</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=5tc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc9 OCA], [https://pdbe.org/5tc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tc9 RCSB], [https://www.ebi.ac.uk/pdbsum/5tc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/G0RVK1_HYPJQ G0RVK1_HYPJQ]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Trichoderma reesei Cel7A efficiently hydrolyses cellulose. We report here the crystallographic structures of the wild-type TrCel7A catalytic domain (CD) in an open state and, for the first time, in a closed state. Molecular dynamics (MD) simulations indicate that the loops along the CD tunnel move in concerted motions. Together, the crystallographic and MD data suggest that the CD cycles between the tense and relaxed forms that are characteristic of work producing enzymes. Analysis of the interactions formed by R251 provides a structural rationale for the concurrent decrease in product inhibition and catalytic efficiency measured for product-binding site mutants.
-Authors:
+Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states.,Bodenheimer AM, Meilleur F FEBS Lett. 2016 Dec;590(23):4429-4438. doi: 10.1002/1873-3468.12464. Epub 2016, Nov 7. PMID:27943301<ref>PMID:27943301</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5tc9" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cellobiohydrolase 3D structures|Cellobiohydrolase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Trichoderma reesei QM6a]]
+[[Category: Bodenheimer AM]]
+[[Category: Meilleur F]]