5XHA

Aspergillus kawachii beta-fructofuranosidase complexed with fructose

Summary for 5XHA

• Entry DOI: 10.2210/pdb5xha/pdb
• Related: 5XH8 5XH9
• Descriptor: Extracellular invertase, beta-D-fructofuranose-(2-1)-beta-D-fructofuranose, SODIUM ION, ... (5 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: 66541.94

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

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: 28715279
DOI: 10.1080/09168451.2017.1353405

Experimental method

X-RAY DIFFRACTION (2.1 Å)