TAILIEUCHUNG - Báo cáo khoa học: Crystal structures of the apo form of b-fructofuranosidase from Bifidobacterium longum and its complex with fructose

We solved the A˚ crystal structure ofb-fructofuranosidase from Bifido-bacterium – a unique enzyme that allows these probiotic bacteria to function in the human digestive system. The sequence ofb-fruc-tofuranosidase classifies it as belonging to the glycoside hydrolase family 32 (GH32). | 1FEBS Journal Crystal structures of the apo form of p-fructofuranosidase from Bifidobacterium longum and its complex with fructose Anna Bujacz Marzena Jedrzejczak-Krzepkowska Stanislaw Bielecki Izabela Redzynia and Grzegorz Bujacz Institute of TechnicalBiochemistry Faculty of Biotechnology and Food Sciences TechnicalUniversity of Lodz Poland Keywords b-fructofuranosidase Bifidobacterium longum crystal structure glycoside hydrolase family GH32 lactic acid bacteria Correspondence A. Bujacz Institute of Technical Biochemistry Faculty of Biotechnology and Food Sciences TechnicalUniversity of Lodz Stefanowskiego 4 10 90-924 Lodz Poland Fax 48 42 6366618 Tel 48 42 6313494 E-mail Received 13 January 2011 revised 25 February 2011 accepted 15 March 2011 doi We solved the A crystal structure of b-fructofuranosidase from Bifidobacterium longum - a unique enzyme that allows these probiotic bacteria to function in the human digestive system. The sequence of b-fruc-tofuranosidase 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 b-propeller and a C-terminal b-sandwich module. The active site is located in the centre of the b-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 b-fructofura-nosidase has a 35-residue elongation of the N-terminus containing a five-turn a-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 A crystal structure of the b-fruc-tofuranosidase complex with

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