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| | <StructureSection load='5xha' size='340' side='right'caption='[[5xha]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5xha' size='340' side='right'caption='[[5xha]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xha]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspkw Aspkw]. 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://proteopedia.org/fgij/fg.htm?mol=5XHA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xha]] 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=5XHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XHA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AKAW_06215 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1033177 ASPKW])</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=5xha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xha OCA], [https://pdbe.org/5xha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xha RCSB], [https://www.ebi.ac.uk/pdbsum/5xha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xha ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G7XM46_ASPKW G7XM46_ASPKW] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspkw]] | + | [[Category: Aspergillus luchuensis IFO 4308]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nagaya, M]] | + | [[Category: Nagaya M]] |
| - | [[Category: Tonozuka, T]] | + | [[Category: Tonozuka T]] |
| - | [[Category: 1-kestose]]
| + | |
| - | [[Category: Beta-propeller]]
| + | |
| - | [[Category: Fructooligosaccharide]]
| + | |
| - | [[Category: Gh32]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
G7XM46_ASPKW
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nagaya M, Kimura M, Gozu Y, Sato S, Hirano K, Tochio T, Nishikawa A, Tonozuka T. Crystal structure of a beta-fructofuranosidase with high transfructosylation activity from Aspergillus kawachii. Biosci Biotechnol Biochem. 2017 Jul 17:1-10. doi: 10.1080/09168451.2017.1353405. PMID:28715279 doi:http://dx.doi.org/10.1080/09168451.2017.1353405
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