6ru2: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ru2 is ON HOLD
+==Crystal Structure of Glucuronoyl Esterase from Cerrena unicolor==
+<StructureSection load='6ru2' size='340' side='right'caption='[[6ru2]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ru2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RU2 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rtv|6rtv]], [[6ru1|6ru1]]</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ru2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ru2 OCA], [http://pdbe.org/6ru2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ru2 RCSB], [http://www.ebi.ac.uk/pdbsum/6ru2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ru2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/GCE_CERUI GCE_CERUI]] Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin (PubMed:25425346, PubMed:26712478).<ref>PMID:25425346</ref> <ref>PMID:26712478</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Structural and functional studies were conducted of the glucuronoyl esterase (GE) from Cerrena unicolor (CuGE), an enzyme catalyzing cleavage of lignin-carbohydrate ester bonds. CuGE is an alpha/beta-hydrolase belonging to carbohydrate esterase family 15 (CE15). The enzyme is modular, comprised of a catalytic and a carbohydrate-binding domain. SAXS data show CuGE as an elongated rigid molecule where the two domains are connected by a rigid linker. Detailed structural information of the catalytic domain in its apo- and inactivated form and complexes with aldouronic acids reveal well-defined binding of the 4-O-methyl-a-D-glucuronoyl moiety, not influenced by the nature of the attached xylo-oligosaccharide. Structural and sequence comparisons within CE15 enzymes reveal two distinct structural subgroups. CuGE belongs to the group of fungal CE15-B enzymes with an open and flat substrate-binding site. The interactions between CuGE and its natural substrates are explained and rationalized by the structural results, microscale thermophoresis and isothermal calorimetry.
-Authors:
+The structural basis of fungal glucuronoyl esterase activity on natural substrates.,Ernst HA, Mosbech C, Langkilde AE, Westh P, Meyer AS, Agger JW, Larsen S Nat Commun. 2020 Feb 24;11(1):1026. doi: 10.1038/s41467-020-14833-9. PMID:32094331<ref>PMID:32094331</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 6ru2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Agger, J W]]
+[[Category: Ernst, H A]]
+[[Category: Langkilde, A]]
+[[Category: Larsen, S]]
+[[Category: Meyer, A]]
+[[Category: Mosbech, C]]
+[[Category: Westh, P]]
+[[Category: Alpha/beta-hydrolase]]
+[[Category: Ce15]]
+[[Category: Esterase]]
+[[Category: Hydrolase]]