2inu: Difference between revisions

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[[Image:2inu.~~jpg~~|left|200px]]

[[Image:2inu.png|left|200px]]

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~~'''~~Crystal structure of inulin fructotransferase in the absence of substrate~~'''~~

===Crystal structure of inulin fructotransferase in the absence of substrate===

~~==Overview==~~

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~~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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_17192265}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17192265 is the PubMed ID number.

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==About this Structure==

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[[Category: Lyase]]

[[Category: Right-handed parallel beta-helix]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jun 18 12~~:15:44 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:14:33 2008''

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-[[Image:2inu.jpg|left|200px]]
+{{Seed}}
+[[Image:2inu.png|left|200px]]
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 {{STRUCTURE_2inu|  PDB=2inu  |  SCENE=  }}
-'''Crystal structure of inulin fructotransferase in the absence of substrate'''
+===Crystal structure of inulin fructotransferase in the absence of substrate===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17192265}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17192265 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17192265}}
 ==About this Structure==
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 [[Category: Lyase]]
 [[Category: Right-handed parallel beta-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:15:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:14:33 2008''