2inv
From Proteopedia
Crystal structure of Inulin fructotransferase in the presence of di-fructose
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedInulin fructotransferase (IFTase), a member of glycoside hydrolase family 91, catalyzes depolymerization of beta-2,1-fructans inulin by successively removing the terminal difructosaccharide units as cyclic anhydrides via intramolecular fructosyl transfer. The crystal structures of IFTase and its substrate-bound complex reveal that IFTase is a trimeric enzyme, and each monomer folds into a right-handed parallel beta-helix. Despite variation in the number and conformation of its beta-strands, the IFTase beta-helix has a structure that is largely reminiscent of other beta-helix structures but is unprecedented in that trimerization is a prerequisite for catalytic activity, and the active site is located at the monomer-monomer interface. Results from crystallographic studies and site-directed mutagenesis provide a structural basis for the exolytic-type activity of IFTase and a functional resemblance to inverting-type glycosyltransferases. Structural and functional insights into intramolecular fructosyl transfer by inulin fructotransferase.,Jung WS, Hong CK, Lee S, Kim CS, Kim SJ, Kim SI, Rhee S J Biol Chem. 2007 Mar 16;282(11):8414-23. Epub 2006 Dec 27. PMID:17192265[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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