1OT2

Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N

1OT2 の概要

• エントリーDOI: 10.2210/pdb1ot2/pdb
• 関連するPDBエントリー: 1OT1 1cdg
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Cyclomaltodextrin glucanotransferase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: glycosyl transferase, 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: 78460.26

構造登録者

Rozeboom, H.J.,Dijkstra, B.W. (登録日: 2003-03-21, 公開日: 2003-06-03, 最終更新日: 2024-10-09)

主引用文献

Leemhuis, H.,Rozeboom, H.J.,Dijkstra, B.W.,Dijkhuizen, L.
The fully conserved Asp residue in Conserved sequence region I of the alpha-amylase Family is crucial for the Catalytic Site Architecture and Activity
Febs Lett., 541:47-51, 2003

PubMed Abstract: The alpha-amylase family is a large group of starch processing enzymes [Svensson, B. (1994) Plant Mol. Biol. 25, 141-157]. It is characterized by four short sequence motifs that contain the seven fully conserved amino acid residues in this family: two catalytic carboxylic acid residues and four substrate binding residues. The seventh conserved residue (Asp135) has no direct interactions with either substrates or products, but it is hydrogen-bonded to Arg227, which does bind the substrate in the catalytic site. Using cyclodextrin glycosyltransferase as an example, this paper provides for the first time definite biochemical and structural evidence that Asp135 is required for the proper conformation of several catalytic site residues and therefore for activity.

PubMed: 12706817
DOI: 10.1016/S0014-5793(03)00286-2

実験手法

X-RAY DIFFRACTION (2.1 Å)