2inv
From Proteopedia
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'''Crystal structure of inulin fructotransferase in the presence of di-fructose''' | '''Crystal structure of inulin fructotransferase in the presence of di-fructose''' | ||
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| + | ==Overview== | ||
| + | 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. | ||
==About this Structure== | ==About this Structure== | ||
2INV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2INV OCA]. | 2INV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2INV OCA]. | ||
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| + | ==Reference== | ||
| + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17192265 17192265] | ||
[[Category: Bacteria]] | [[Category: Bacteria]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jung, W S.]] | [[Category: Jung, W S.]] | ||
[[Category: Rhee, S.]] | [[Category: Rhee, S.]] | ||
| + | [[Category: Lyase]] | ||
[[Category: Protein-carbohydrate complex]] | [[Category: Protein-carbohydrate complex]] | ||
[[Category: Right-handed parallel beta-helix]] | [[Category: Right-handed parallel beta-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:15:44 2008'' |
Revision as of 09:15, 18 June 2008
Crystal structure of inulin fructotransferase in the presence of di-fructose
Overview
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.
About this Structure
2INV is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Wed Jun 18 12:15:44 2008
