View source for 5xh8


==Aspergillus kawachii beta-fructofuranosidase complexed with glycerol==
<StructureSection load='5xh8' size='340' side='right'caption='[[5xh8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xh8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_luchuensis_IFO_4308 Aspergillus luchuensis IFO 4308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XH8 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5xh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xh8 OCA], [https://pdbe.org/5xh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xh8 RCSB], [https://www.ebi.ac.uk/pdbsum/5xh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xh8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G7XM46_ASPKW G7XM46_ASPKW] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Fructofuranosidases belonging to glycoside hydrolase family (GH) 32 are enzymes that hydrolyze sucrose. Some GH32 enzymes also catalyze transfructosylation to produce fructooligosaccharides. We found that Aspergillus kawachii IFO 4308 beta-fructofuranosidase (AkFFase) produces fructooligosaccharides, mainly 1-kestose, from sucrose. We determined the crystal structure of AkFFase. AkFFase is composed of an N-terminal small component, a beta-propeller catalytic domain, an alpha-helical linker, and a C-terminal beta-sandwich, similar to other GH32 enzymes. AkFFase forms a dimer, and the dimerization pattern is different from those of other oligomeric GH32 enzymes. The complex structure of AkFFase with fructose unexpectedly showed that fructose binds both subsites -1 and +1, despite the fact that the catalytic residues were not mutated. Fructose at subsite +1 interacts with Ile146 and Glu296 of AkFFase via direct hydrogen bonds.

Crystal structure of a beta-fructofuranosidase with high transfructosylation activity from Aspergillus kawachii.,Nagaya M, Kimura M, Gozu Y, Sato S, Hirano K, Tochio T, Nishikawa A, Tonozuka T Biosci Biotechnol Biochem. 2017 Jul 17:1-10. doi: 10.1080/09168451.2017.1353405. PMID:28715279<ref>PMID:28715279</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xh8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Invertase|Invertase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus luchuensis IFO 4308]]
[[Category: Large Structures]]
[[Category: Nagaya M]]
[[Category: Tonozuka T]]