5A2C

Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass

5A2C の概要

• エントリーDOI: 10.2210/pdb5a2c/pdb
• 関連するPDBエントリー: 5A2A 5A2B
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: ALPHA-AMYLASE, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, calcium-binding site, geobacillus, glycosyl hydrolase
• 由来する生物種: ANOXYBACILLUS SP.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58667.01

構造登録者

Ng, C.L.,Chai, K.P.,Othman, N.F.,Teh, A.H.,Ho, K.L.,Chan, K.G.,Goh, K.M. (登録日: 2015-05-17, 公開日: 2016-03-30, 最終更新日: 2024-01-10)

主引用文献

Chai, K.P.,Othman, N.F.B.,Teh, A.,Ho, K.L.,Chan, K.,Shamsir, M.S.,Goh, K.M.,Ng, C.L.
Crystal Structure of Anoxybacillus Alpha-Amylase Provides Insights Into Maltose Binding of a New Glycosyl Hydrolase Subclass.
Sci.Rep., 6:23126-, 2016

PubMed Abstract: A new subfamily of glycosyl hydrolase family GH13 was recently proposed for α-amylases from Anoxybacillus species (ASKA and ADTA), Geobacillus thermoleovorans (GTA, Pizzo, and GtamyII), Bacillus aquimaris (BaqA), and 95 other putative protein homologues. To understand this new GH13 subfamily, we report crystal structures of truncated ASKA (TASKA). ASKA is a thermostable enzyme capable of producing high levels of maltose. Unlike GTA, biochemical analysis showed that Ca(2+) ion supplementation enhances the catalytic activities of ASKA and TASKA. The crystal structures reveal the presence of four Ca(2+) ion binding sites, with three of these binding sites are highly conserved among Anoxybacillus α-amylases. This work provides structural insights into this new GH13 subfamily both in the apo form and in complex with maltose. Furthermore, structural comparison of TASKA and GTA provides an overview of the conformational changes accompanying maltose binding at each subsite.

PubMed: 26975884
DOI: 10.1038/SREP23126

実験手法

X-RAY DIFFRACTION (1.9 Å)