View source for 9tdu


==Structure of Fructofuranosidase from Purpureocilum lilacinum==
<StructureSection load='9tdu' size='340' side='right'caption='[[9tdu]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9tdu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_phaffii_CBS_7435 Komagataella phaffii CBS 7435]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9TDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9TDU 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]] 2.1&#8491;</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9tdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9tdu OCA], [https://pdbe.org/9tdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9tdu RCSB], [https://www.ebi.ac.uk/pdbsum/9tdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9tdu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A179H0Q0_PURLI A0A179H0Q0_PURLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Fructofuranosidases are key biocatalysts in the synthesis of fructooligosaccharides (FOS), prebiotics whose biological properties depend on the specific arrangement of beta-(2 --&gt; 1) and/or beta-(2 --&gt; 6) fructosyl linkages. Tailoring FOS structures therefore requires enzymes with adjustable specificities. In this work, we characterize the structural and functional features of the novel beta-fructofuranosidase PlINV from Purpureocillium lilacinum, aiming to enhance its utility in the production of bioactive compounds. Purified PlINV exhibits broad substrate specificity, preferring sucrose but also acting on fructose-based polymers with diverse linkage types. It displays wide acceptor promiscuity in transfructosylation reactions, generating several trisaccharides from sucrose. The three-dimensional structure, solved at 2.1 A, reveals a previously unreported tetrameric assembly within the GH32 family and a relatively occluded active site. Structures of various enzyme-substrate complexes identify residues governing substrate recognition and highlight substantial conformational plasticity, including numerous water-mediated interactions. Structure-guided mutagenesis within the active-site cleft generated variants with altered hydrolytic activity and distinct FOS profiles, confirming the functional importance of the identified residues. Substitutions Q259A and P207N increased overall FOS yield, whereas N289T selectively enriched neokestose within a broader product mixture. PlINV also efficiently fructosylated the polyphenols hydroxytyrosol and piceid-this latter reaction being described for the first time-validated by HPLC-MS analyses. Docking simulations suggest that polyphenol accommodation relies mainly on hydrophobic contacts, complemented by limited polar interactions. Collectively, these results provide a robust structural and mechanistic framework for engineering PlINV to fine-tune its biocatalytic properties, enabling the targeted production of specific FOS and other bioactive compounds for biotechnological applications.

Structural and mechanistic insights into a novel beta-fructofuranosidase from Purpureocillium lilacinum with high transfructosylating activity and an atypical tetrameric assembly.,Narmontaite E, Ruiz-Nunez M, Plou FJ, Fernandez-Lobato M, Sanz-Aparicio J Int J Biol Macromol. 2026 Feb;345:150552. doi: 10.1016/j.ijbiomac.2026.150552. , Epub 2026 Jan 28. PMID:41617004<ref>PMID:41617004</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9tdu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Komagataella phaffii CBS 7435]]
[[Category: Large Structures]]
[[Category: Ruiz-Nunez M]]
[[Category: Sanz-Aparicio J]]