1cxk
From Proteopedia
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[[Image:1cxk.gif|left|200px]] | [[Image:1cxk.gif|left|200px]] | ||
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'''COMPLEX BETWEEN A MALTONONAOSE SUBSTRATE AND BACILLUS CIRCULANS STRAIN 251 CGTASE E257Q/D229N''' | '''COMPLEX BETWEEN A MALTONONAOSE SUBSTRATE AND BACILLUS CIRCULANS STRAIN 251 CGTASE E257Q/D229N''' | ||
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[[Category: Kalk, K H.]] | [[Category: Kalk, K H.]] | ||
[[Category: Uitdehaag, J C.M.]] | [[Category: Uitdehaag, J C.M.]] | ||
- | [[Category: | + | [[Category: Alpha-amylase family]] |
- | [[Category: | + | [[Category: Glycosyl hydrolase family 13]] |
- | [[Category: | + | [[Category: Maltononaose]] |
- | [[Category: | + | [[Category: Substrate complex]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:13:14 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 10:13, 2 May 2008
COMPLEX BETWEEN A MALTONONAOSE SUBSTRATE AND BACILLUS CIRCULANS STRAIN 251 CGTASE E257Q/D229N
Overview
Cyclodextrin glycosyltransferase (CGTase) is an enzyme of the alpha-amylase family, which uses a double displacement mechanism to process alpha-linked glucose polymers. We have determined two X-ray structures of CGTase complexes, one with an intact substrate at 2.1 A resolution, and the other with a covalently bound reaction intermediate at 1.8 A resolution. These structures give evidence for substrate distortion and the covalent character of the intermediate and for the first time show, in atomic detail, how catalysis in the alpha-amylase family proceeds by the concerted action of all active site residues.
About this Structure
1CXK is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.
Reference
X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family., Uitdehaag JC, Mosi R, Kalk KH, van der Veen BA, Dijkhuizen L, Withers SG, Dijkstra BW, Nat Struct Biol. 1999 May;6(5):432-6. PMID:10331869 Page seeded by OCA on Fri May 2 13:13:14 2008