6M0D

Beijerinckia indica beta-fructosyltransferase

Summary for 6M0D

• Entry DOI: 10.2210/pdb6m0d/pdb
• Descriptor: Levansucrase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: gh68, fructooligosaccharide, hydrolase
• Biological source: Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
• Total number of polymer chains: 1
• Total formula weight: 57053.40

Authors

Tonozuka, T. (deposition date: 2020-02-21, release date: 2020-08-12, Last modification date: 2023-11-29)

Primary citation

Tonozuka, T.,Kitamura, J.,Nagaya, M.,Kawai, R.,Nishikawa, A.,Hirano, K.,Tamura, K.,Fujii, T.,Tochio, T.
Crystal structure of a glycoside hydrolase family 68 beta-fructosyltransferase from Beijerinckia indica subsp. indica in complex with fructose.
Biosci.Biotechnol.Biochem., 84:2508-2520, 2020

PubMed Abstract: An enzyme belonging to glycoside hydrolase family 68 (GH68) from subsp. NBRC 3744 was expressed in . Biochemical characterization showed that the enzyme was identified to be a β-fructosyltransferase (BiBftA). Crystallization of a full-length BiBftA was initially attempted, but no crystals were obtained. We constructed a variant in which 5 residues (Pro199-Gly203) and 13 residues (Leu522-Gln534) in potentially flexible regions were deleted, and we successfully crystallized this variant BiBftA. BiBftA is composed of a five-bladed β-propeller fold as in other GH68 enzymes. The structure of BiBftA in complex with fructose unexpectedly indicated that one β-fructofuranose (β-Fru) molecule and one β-fructopyranose molecule bind to the catalytic pocket. The orientation of β-Fru at subsite -1 is tilted from the orientation observed in most GH68 enzymes, presenting a second structure of a GH68 enzyme in complex with the tilted binding mode of β-Fru

PubMed: 32752982
DOI: 10.1080/09168451.2020.1804317

Experimental method

X-RAY DIFFRACTION (2.2 Å)