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1d3c

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{{STRUCTURE_1d3c| PDB=1d3c | SCENE= }}
{{STRUCTURE_1d3c| PDB=1d3c | SCENE= }}
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'''MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN'''
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===MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN===
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==Overview==
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The enzyme cyclodextrin glycosyltransferase is closely related to alpha-amylases but has the unique ability to produce cyclodextrins (circular alpha(1--&gt;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.
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{{ABSTRACT_PUBMED_10574960}}
==About this Structure==
==About this Structure==
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[[Category: Product complex]]
[[Category: Product complex]]
[[Category: Transglycosylation]]
[[Category: Transglycosylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:24:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:17:28 2008''

Revision as of 19:17, 30 June 2008

Image:1d3c.png

Template:STRUCTURE 1d3c

MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN

Template:ABSTRACT PUBMED 10574960

About this Structure

1D3C is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution., Uitdehaag JC, Kalk KH, van Der Veen BA, Dijkhuizen L, Dijkstra BW, J Biol Chem. 1999 Dec 3;274(49):34868-76. PMID:10574960

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