View source for 5yqs


==Isoprimeverose-producing enzyme from Aspergillus oryzae in complex with isoprimeverose==
<StructureSection load='5yqs' size='340' side='right'caption='[[5yqs]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yqs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_oryzae_RIB40 Aspergillus oryzae RIB40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YQS 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</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=5yqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yqs OCA], [https://pdbe.org/5yqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yqs RCSB], [https://www.ebi.ac.uk/pdbsum/5yqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yqs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2U8V9_ASPOR Q2U8V9_ASPOR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Isoprimeverose-producing enzymes (IPases) release isoprimeverose (alpha-d-xylopyranosyl-(1--&gt;6)-d-glucopyranose) from the non-reducing end of xyloglucan oligosaccharides. Aspergillus oryzae IPase (IpeA) is classified as a member of the glycoside hydrolase family 3 (GH3); however, it has unusual substrate specificity compared with other GH3 enzymes. Xylopyranosyl branching at the non-reducing ends of xyloglucan oligosaccharides is vital for IpeA activity. We solved the crystal structure of IpeA with isoprimeverose at 2.4A resolution, showing that the structure of IpeA formed a dimer and was composed of three domains: an N-terminal (beta/alpha)8 TIM-barrel domain, alpha/beta/alpha sandwich fold domain, and a C-terminal fibronectin-like domain. The catalytic TIM-barrel domain possessed a catalytic nucleophile (Asp300) and acid/base (Glu524) residues. Interestingly, we found that the cavity of the active site of IpeA was larger than that of other GH3 enzymes, and subsite -1' played an important role in its activity. The glucopyranosyl and xylopyranosyl residues of isoprimeverose were located at subsites -1 and -1', respectively. Gln58 and Tyr89 contributed to the interaction with the xylopyranosyl residue of isoprimeverose through hydrogen bonding and stacking effects, respectively. Our findings provide new insights into the substrate recognition of GH3 enzymes.

Crystal structure and substrate recognition mechanism of Aspergillus oryzae isoprimeverose-producing enzyme.,Matsuzawa T, Watanabe M, Nakamichi Y, Fujimoto Z, Yaoi K J Struct Biol. 2019 Jan 1;205(1):84-90. doi: 10.1016/j.jsb.2018.11.005. Epub 2018, Nov 13. PMID:30445155<ref>PMID:30445155</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yqs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus oryzae RIB40]]
[[Category: Large Structures]]
[[Category: Matsuzawa T]]
[[Category: Nakamichi Y]]
[[Category: Watanabe M]]
[[Category: Yaoi K]]