2inu | pdb_00002inu

Crystal structure of Inulin fructotransferase in the absence of substrate

spinqualitylabelsall models 2inu, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2inu is a 3 chain structure with sequence from Bacillus sp. snu-7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: 2PO, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3SAG3_9BACI Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Inulin 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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