3pic

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<StructureSection load='3pic' size='340' side='right'caption='[[3pic]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3pic' size='340' side='right'caption='[[3pic]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pic]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pic]] is a 3 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=3PIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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]] 1.9&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=3pic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pic OCA], [https://pdbe.org/3pic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pic RCSB], [https://www.ebi.ac.uk/pdbsum/3pic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pic ProSAT]</span></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=3pic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pic OCA], [https://pdbe.org/3pic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pic RCSB], [https://www.ebi.ac.uk/pdbsum/3pic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pic ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CIP2_HYPJQ CIP2_HYPJQ]] 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. Does not hydrolyze substrates of other carbohydrate esterases such as acetylxylan esterase, acetyl esterase and feruloyl esterase.<ref>PMID:12788920</ref> <ref>PMID:17678650</ref>
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[https://www.uniprot.org/uniprot/GCE_HYPJQ GCE_HYPJQ] 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. Does not hydrolyze substrates of other carbohydrate esterases such as acetylxylan esterase, acetyl esterase and feruloyl esterase.<ref>PMID:12788920</ref> <ref>PMID:17678650</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of the catalytic domain of glucuronoyl esterase Cip2 from the fungus H. jecorina was determined at a resolution of 1.9 A. This is the first structure of the newly established carbohydrate esterase family 15. The structure has revealed the residues Ser278-His411-Glu301 present in a triad arrangement as the active site. Ser278 is present in the novel consensus sequence GCSRXG reported earlier in the members of CE-15 family. The active site is exposed on the surface of the protein which has implications for the ability of the enzyme to hydrolyze ester bonds of large substrates. Efforts are underway to obtain crystals of Cip2_GE complexed with inhibitor and synthetic substrates. The activity of the glucuronoyl esterase could play a significant role in plant biomass degradation as its expected role is to separate the lignin from hemicelluloses by hydrolysis of the ester bond between 4-O-methyl-D-glucuronic acid moieties of glucuronoxylans and aromatic alcohols of lignin.
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Structure of the catalytic domain of glucuronoyl esterase Cip2 from Hypocrea jecorina.,Pokkuluri PR, Duke NE, Wood SJ, Cotta MA, Li XL, Biely P, Schiffer M Proteins. 2011 Aug;79(8):2588-92. doi: 10.1002/prot.23088. Epub 2011 Jun 9. PMID:21661060<ref>PMID:21661060</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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<div class="pdbe-citations 3pic" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hypocrea jecorina]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pokkuluri, P R]]
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[[Category: Trichoderma reesei]]
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[[Category: Alpha/beta hydrolase fold]]
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[[Category: Pokkuluri PR]]
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[[Category: Glucuronoyl esterase]]
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[[Category: Hydrolase]]
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[[Category: N-linked glycosylation]]
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[[Category: Secreted]]
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Revision as of 13:31, 1 March 2024

Glucuronoyl Esterase catalytic domain (Cip2_GE) from Hypocrea jecorina

PDB ID 3pic

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