9CGT

STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE COMPLEXED WITH A THIO-MALTOPENTAOSE

9CGT の概要

• エントリーDOI: 10.2210/pdb9cgt/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900100
• 分子名称: PROTEIN (CYCLODEXTRIN-GLYCOSYLTRANSFERASE), alpha-D-glucopyranose-(1-4)-4-thio-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-4-thio-alpha-D-glucopyranose-(1-4)-1-thio-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: glycosyltransferase, starch degradation, cyclodextrin, transferase
• 由来する生物種: Bacillus circulans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 75464.08

構造登録者

Schmidt, A.K.,Schulz, G.E. (登録日: 1998-09-27, 公開日: 1998-10-14, 最終更新日: 2024-10-30)

主引用文献

Parsiegla, G.,Schmidt, A.K.,Schulz, G.E.
Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production.
Eur.J.Biochem., 255:710-717, 1998

PubMed Abstract: Bacterial cyclodextrin glycosyltransferases use starch to produce cyclic maltooligosaccharides (cyclodextrins) which are of interest in various applications. The cyclization reaction gives rise to a spectrum of ring sizes consisting of predominantly six to eight glucosyl units. Using the enzyme from Bacillus circulans strain no. 8, binding studies have been performed with several substrates and analogues. The observed binding modes differ in detail, but agree in general with data on homologous enzymes. Based on these binding studies, two mutations were designed that changed the production spectrum from the predominant product beta-cyclodextrin of the wild-type enzyme towards gamma-cyclodextrin, which is of practical interest because it is rare and can encapsulate larger nonpolar compounds.

PubMed: 9738912
DOI: 10.1046/j.1432-1327.1998.2550710.x

実験手法

X-RAY DIFFRACTION (2.5 Å)