1DED

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

1DED の概要

• エントリーDOI: 10.2210/pdb1ded/pdb
• 関連するPDBエントリー: 1D7F 1PAM
• 関連するBIRD辞書のPRD_ID: PRD_900022
• 分子名称: 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)
• 機能のキーワード: cyclodextrin glucanotransferase, cgtase, acarbose, transferase
• 由来する生物種: Bacillus sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 152509.21

構造登録者

Ishii, N.,Haga, K.,Yamane, K.,Harata, K. (登録日: 1999-11-14, 公開日: 2000-04-07, 最終更新日: 2024-10-09)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2 Å)