5xh9: Difference between revisions

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'''Unreleased structure'''


The entry 5xh9 is ON HOLD  until Paper Publication
==Aspergillus kawachii beta-fructofuranosidase==
<StructureSection load='5xh9' size='340' side='right' caption='[[5xh9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xh9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XH9 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xh8|5xh8]], [[5xha|5xha]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xh9 OCA], [http://pdbe.org/5xh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xh9 RCSB], [http://www.ebi.ac.uk/pdbsum/5xh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xh9 ProSAT]</span></td></tr>
</table>
<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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5xh9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Nagaya, M]]
[[Category: Tonozuka, T]]
[[Category: 1-kestose]]
[[Category: Beta-propeller]]
[[Category: Fructooligosaccharide]]
[[Category: Gh32]]
[[Category: Hydrolase]]
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