2INU
Crystal structure of Inulin fructotransferase in the absence of substrate
Summary for 2INU
| Entry DOI | 10.2210/pdb2inu/pdb |
| Related | 2INV |
| Descriptor | Inulin fructotransferase, PHOSPHONATE (3 entities in total) |
| Functional Keywords | right-handed parallel beta-helix, lyase |
| Biological source | Bacillus sp. snu-7 |
| Total number of polymer chains | 3 |
| Total formula weight | 130950.52 |
| Authors | Rhee, S.,Jung, W.S. (deposition date: 2006-10-09, release date: 2006-12-26, Last modification date: 2024-10-16) |
| Primary citation | Jung, W.S.,Hong, C.K.,Lee, S.,Kim, C.S.,Kim, S.J.,Kim, S.I.,Rhee, S. Structural and functional insights into intramolecular fructosyl transfer by Inulin fructotransferase J.Biol.Chem., 282:8414-8423, 2007 Cited by PubMed Abstract: 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. PubMed: 17192265DOI: 10.1074/jbc.M607143200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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