1JL8

Complex of alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with beta-cyclodextrin based on a co-crystallization with methyl beta-cyclodextrin

1JL8 の概要

• エントリーDOI: 10.2210/pdb1jl8/pdb
• 関連するPDBエントリー: 1BVZ 1G1Y 1JIB
• 関連するBIRD辞書のPRD_ID: PRD_900012
• 分子名称: ALPHA-AMYLASE II, Cycloheptakis-(1-4)-(alpha-D-glucopyranose) (2 entities in total)
• 機能のキーワード: pullulan, cyclodextrin, neopullulanase, methyl beta-cyclodextrin, beta-cyclodextrin, hydrolase
• 由来する生物種: Thermoactinomyces vulgaris
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 137412.25

構造登録者

Yokota, T.,Tonozuka, T.,Shimura, Y.,Ichikawa, K.,Kamitori, S.,Sakano, Y. (登録日: 2001-07-16, 公開日: 2001-08-01, 最終更新日: 2023-10-25)

主引用文献

Yokota, T.,Tonozuka, T.,Shimura, Y.,Ichikawa, K.,Kamitori, S.,Sakano, Y.
Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
Biosci.Biotechnol.Biochem., 65:619-626, 2001

PubMed Abstract: The structures of Thermoactinomyces vulgaris R-47 alpha-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl beta-cyclodextrin (m beta-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2 A and 3.3 A resolution, respectively. In d325nTVA II-m beta-CD complex, the orientation and binding-position of beta-CD in TVA II were identical to those in cyclodextin glucanotransferase (CGTase). The active site residues were essentialy conserved, while there are no residues corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In d325nTVA II-G6 complex, the electron density maps of two glucosyl units at the non-reducing end were disordered and invisible. The four glucosyl units of G6 were bound to TVA II as in CGTase, while the others were not stacked and were probably flexible. The residues of TVA II corresponding to Tyr89, Lys232, and His233 of CGTase were completely lacking. These results suggest that the lack of the residues related to alpha-glucan and CD-stacking causes the functional distinctions between CGTase and TVA II.

PubMed: 11330677
DOI: 10.1271/bbb.65.619

実験手法

X-RAY DIFFRACTION (3.2 Å)