Literature summary for 4.2.2.16 extracted from

Park, J.; Kim, M.I.; Park, Y.D.; Shin, I.; Cha, J.; Kim, C.H.; Rhee, S.
Structural and functional basis for substrate specificity and catalysis of levan fructotransferase (2012), J. Biol. Chem., 287, 31233-31241.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in apo form, as well as in complexes with sucrose and levanbiose. Enzyme contains an active site that accommodates a difructosaccharide using the -1 and -2 subsites. Binding is facilitated by small side chain residues in the loop region of a catalytic beta-propeller N-domain. An additional oligosaccharide-binding site is in the beta-sandwich C-domain, supporting its role in carbohydrate recognition	Paenarthrobacter ureafaciens

Crystallization (Comment)

Organism

in apo form, as well as in complexes with sucrose and levanbiose. Enzyme contains an active site that accommodates a difructosaccharide using the -1 and -2 subsites. Binding is facilitated by small side chain residues in the loop region of a catalytic beta-propeller N-domain. An additional oligosaccharide-binding site is in the beta-sandwich C-domain, supporting its role in carbohydrate recognition

Paenarthrobacter ureafaciens

Protein Variants

Protein Variants	Comment	Organism
D54N	inactive mutant, used for the structural analysis of the complex with sucrose	Paenarthrobacter ureafaciens

Organism

Organism	UniProt	Comment	Textmining
Paenarthrobacter ureafaciens	Q9KJD0	-	-

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Release 2023.1 (January 2023)