1DED
CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION
Summary for 1DED
Entry DOI | 10.2210/pdb1ded/pdb |
Related | 1D7F 1PAM |
Related PRD ID | PRD_900022 |
Descriptor | CYCLODEXTRIN 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 Keywords | cyclodextrin glucanotransferase, cgtase, acarbose, transferase |
Biological source | Bacillus sp. |
Total number of polymer chains | 2 |
Total formula weight | 152509.21 |
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 citation | Ishii, 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: 10731709PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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