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1DED

CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION

Summary for 1DED
Entry DOI10.2210/pdb1ded/pdb
Related1D7F 1PAM
Related PRD IDPRD_900022
DescriptorCYCLODEXTRIN GLUCANOTRANSFERASE, 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
Functional Keywordscyclodextrin glucanotransferase, cgtase, acarbose, transferase
Biological sourceBacillus sp.
Total number of polymer chains2
Total formula weight152509.21
Authors
Ishii, N.,Haga, K.,Yamane, K.,Harata, K. (deposition date: 1999-11-14, release date: 2000-04-07, Last modification date: 2024-10-09)
Primary citationIshii, N.,Haga, K.,Yamane, K.,Harata, K.
Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution.
J.Biochem.(Tokyo), 127:383-391, 2000
Cited by
PubMed Abstract: The product specificity of cyclodextrin glucanotransferase (CGTase) from alkalophilic Bacillus sp. #1011 is improved to near-uniformity by mutation of histidine-233 to asparagine. Asparagine 233-replaced CGTase (H233N-CGTase) no longer produces alpha-cyclodextrin, while the wild-type CGTase from the same bacterium produces a mixture of predominantly alpha-, beta-, and gamma-cyclodextrins, catalyzing the conversion of starch into cyclic or linear alpha-1,4-linked glucopyranosyl chains. In order to better understand the protein engineering of H233N-CGTase, the crystal structure of the mutant enzyme complexed with a maltotetraose analog, acarbose, was determined at 2.0 A resolution with a final crystallographic R value of 0.163 for all data. Taking a close look at the active site cleft in which the acarbose molecule is bound, the most probable reason for the improved specificity of H233N-CGTase is the removal of interactions needed to form a compact ring like a-cyclodextrin.
PubMed: 10731709
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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