5XH9
Aspergillus kawachii beta-fructofuranosidase
Summary for 5XH9
| Entry DOI | 10.2210/pdb5xh9/pdb |
| Related | 5XH8 5XHA |
| Descriptor | Extracellular invertase, SODIUM ION (3 entities in total) |
| Functional Keywords | fructooligosaccharides, 1-kestose, gh32, beta-propeller, hydrolase |
| Biological source | Aspergillus kawachii (strain NBRC 4308) (White koji mold) |
| Total number of polymer chains | 1 |
| Total formula weight | 65839.33 |
| Authors | Nagaya, M.,Tonozuka, T. (deposition date: 2017-04-19, release date: 2017-07-19, Last modification date: 2023-11-22) |
| Primary citation | 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., 81:1786-1795, 2017 Cited by PubMed Abstract: β-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 β-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 β-propeller catalytic domain, an α-helical linker, and a C-terminal β-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. PubMed: 28715279DOI: 10.1080/09168451.2017.1353405 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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