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3sc7
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.== | |
| + | <StructureSection load='3sc7' size='340' side='right'caption='[[3sc7]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3sc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_ficuum Aspergillus ficuum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SC7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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"><div style='overflow: auto; max-height: 3em;'>[[3rwk|3rwk]]</div></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Inulinase Inulinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.7 3.2.1.7] </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=3sc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sc7 OCA], [https://pdbe.org/3sc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sc7 RCSB], [https://www.ebi.ac.uk/pdbsum/3sc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sc7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/INU2_ASPFI INU2_ASPFI]] Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60.<ref>PMID:24251113</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Endo-inulinase is a member of glycosidase hydrolase family 32 (GH32) degrading fructans of the inulin type with an endo-cleavage mode and is an important class of industrial enzyme. In the present study, we report the first crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum at 1.5 A. It was solved by molecular replacement with the structure of exo-inulinase as search model. The 3D structure presents a bimodular arrangement common to other GH32 enzymes: a N-terminal 5-fold beta-propeller catalytic domain with four beta-sheets and a C-terminal beta-sandwich domain organized in two beta-sheets with five beta-strands. The structural analysis and comparison with other GH32 enzymes reveal the presence of an extra pocket in the INU2 catalytic site, formed by two loops and the conserved motif W-M(I)-N-D(E)-P-N-G. This cavity would explain the endo-activity of the enzyme, the critical role of Trp40 and particularly the cleavage at the third unit of the inulin(-like) substrates. Crystal structure at 2.1 A of INU2 complexed with fructosyl molecules, experimental digestion data and molecular modelling studies support these hypotheses. | ||
| - | + | First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: Discovery of an extra-pocket in the catalytic domain responsible for its endo-activity.,Pouyez J, Mayard A, Vandamme AM, Roussel G, Perpete EA, Wouters J, Housen I, Michaux C Biochimie. 2012 Jun 28. PMID:22750808<ref>PMID:22750808</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3sc7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus ficuum]] | ||
| + | [[Category: Inulinase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Housen, I]] | ||
| + | [[Category: Mayard, A]] | ||
| + | [[Category: Michaux, C]] | ||
| + | [[Category: Pouyez, J]] | ||
| + | [[Category: Roussel, G]] | ||
| + | [[Category: Vandamme, A M]] | ||
| + | [[Category: Wouters, J]] | ||
| + | [[Category: Cytosol]] | ||
| + | [[Category: Endo-inulinase]] | ||
| + | [[Category: Glycoside hydrolase family 32]] | ||
| + | [[Category: Glycosylation]] | ||
| + | [[Category: Hydrolase]] | ||
Current revision
First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.
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