1PJ9

Bacillus circulans strain 251 loop mutant 183-195

1PJ9 の概要

• エントリーDOI: 10.2210/pdb1pj9/pdb
• 関連するPDBエントリー: 1CDG
• 関連するBIRD辞書のPRD_ID: PRD_900001 PRD_900009
• 分子名称: Cyclomaltodextrin glucanotransferase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: glycosyltransferase, transferase, cyclodextrin
• 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: 77283.95

構造登録者

Rozeboom, H.J.,Dijkstra, B.W. (登録日: 2003-06-02, 公開日: 2004-02-03, 最終更新日: 2024-11-06)

主引用文献

Leemhuis, H.,Rozeboom, H.J.,Dijkstra, B.W.,Dijkhuizen, L.
Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge
PROTEINS: STRUCT.,FUNCT.,GENET., 54:128-134, 2004

PubMed Abstract: Cyclodextrin glycosyltransferase (CGTase) catalyzes the formation of cyclodextrins from starch. Among the CGTases with known three-dimensional structure, Thermoanaerobacterium thermosulfurigenes CGTase has the highest thermostability. By replacing amino acid residues in the B-domain of Bacillus circulans CGTase with those from T. thermosulfurigenes CGTase, we identified a B. circulans CGTase mutant (with N188D and K192R mutations), with a strongly increased activity half-life at 60 degrees C. Asp188 and Arg192 form a salt bridge in T. thermosulfurigenes CGTase. Structural analysis of the B. circulans CGTase mutant revealed that this salt bridge is also formed in the mutant. Thus, the activity half-life of this enzyme can be enhanced by rational protein engineering.

PubMed: 14705029
DOI: 10.1002/prot.10516

実験手法

X-RAY DIFFRACTION (2 Å)