5xha: Difference between revisions
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==Aspergillus kawachii beta-fructofuranosidase complexed with fructose== | |||
<StructureSection load='5xha' size='340' side='right' caption='[[5xha]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5xha]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XHA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XHA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <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]], [[5xh9|5xh9]]</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=5xha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xha OCA], [http://pdbe.org/5xha PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xha RCSB], [http://www.ebi.ac.uk/pdbsum/5xha PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xha 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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5xha" 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]] | |||
Revision as of 04:04, 4 August 2017
Aspergillus kawachii beta-fructofuranosidase complexed with fructose
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