3pig

Publication Abstract from PubMed

We solved the 1.8 A crystal structure of beta-fructofuranosidase from Bifidobacterium longum KN29.1 - a unique enzyme that allows these probiotic bacteria to function in the human digestive system. The sequence of beta-fructofuranosidase classifies it as belonging to the glycoside hydrolase family 32 (GH32). GH32 enzymes show a wide range of substrate specificity and different functions in various organisms. All enzymes from this family share a similar fold, containing two domains: an N-terminal five-bladed beta-propeller and a C-terminal beta-sandwich module. The active site is located in the centre of the beta-propeller domain, in the bottom of a 'funnel'. The binding site, -1, responsible for tight fructose binding, is highly conserved among the GH32 enzymes. Bifidobacterium longum KN29.1 beta-fructofuranosidase has a 35-residue elongation of the N-terminus containing a five-turn alpha-helix, which distinguishes it from the other known members of the GH32 family. This new structural element could be one of the functional modifications of the enzyme that allows the bacteria to act in a human digestive system. We also solved the 1.8 A crystal structure of the beta-fructofuranosidase complex with beta-d-fructose, a hydrolysis product obtained by soaking apo crystal in raffinose. Database Coordinates and structure factors have been deposited in the Protein Data Bank under accession codes: 3PIG and 3PIJ Structured digital abstract * -fructofuranosidase binds to -fructofuranosidase by x-ray crystallography (View interaction).

Crystal structures of the apo form of beta-fructofuranosidase from Bifidobacterium longum and its complex with fructose.,Bujacz A, Jedrzejczak-Krzepkowska M, Bielecki S, Redzynia I, Bujacz G FEBS J. 2011 Mar 18. doi: 10.1111/j.1742-4658.2011.08098.x. PMID:21418142^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.