Linked Life Data

10574960

Source:http://linkedlifedata.com/resource/pubmed/id/10574960

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pubmed-article:10574960pubmed:abstractTextThe enzyme cyclodextrin glycosyltransferase is closely related to alpha-amylases but has the unique ability to produce cyclodextrins (circular alpha(1-->4)-linked glucoses) from starch. To characterize this specificity we determined a 1.8-A structure of an E257Q/D229N mutant cyclodextrin glycosyltransferase in complex with its product gamma-cyclodextrin, which reveals for the first time how cyclodextrin is competently bound. Across subsites -2, -1, and +1, the cyclodextrin ring binds in a twisted mode similar to linear sugars, giving rise to deformation of its circular symmetry. At subsites -3 and +2, the cyclodextrin binds in a manner different from linear sugars. Sequence comparisons and site-directed mutagenesis experiments support the conclusion that subsites -3 and +2 confer the cyclization activity in addition to subsite -6 and Tyr-195. On this basis, a role of the individual residues during the cyclization reaction cycle is proposed.lld:pubmed
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pubmed-article:10574960pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:10574960pubmed:articleTitleThe cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution.lld:pubmed
pubmed-article:10574960pubmed:affiliationBIOSON Research Institute, Laboratory of Biophysical Chemistry, Groningen Biomolecular Sciences, University of Groningen, Nijenborgh 4, 9747AG Groningen, the Netherlands.lld:pubmed
pubmed-article:10574960pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10574960pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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