1MWO

Crystal Structure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase

1MWO の概要

• エントリーDOI: 10.2210/pdb1mwo/pdb
• 関連するPDBエントリー: 1MXD 1MXG
• 分子名称: alpha amylase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: (beta/alpha)8-barrel, alpha-amylase, hydrolase
• 由来する生物種: Pyrococcus woesei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50661.21

構造登録者

Linden, A.,Mayans, O.,Meyer-Klaucke, W.,Antranikian, G.,Wilmanns, M. (登録日: 2002-09-30, 公開日: 2003-06-10, 最終更新日: 2024-11-06)

主引用文献

Linden, A.,Mayans, O.,Meyer-Klaucke, W.,Antranikian, G.,Wilmanns, M.
Differential Regulation of a Hyperthermophilic alpha-Amylase with a Novel (Ca,Zn) Two-metal Center by Zinc
J.Biol.Chem., 278:9875-9884, 2003

PubMed Abstract: The crystal structure of the alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei was solved in the presence of three inhibitors: acarbose, Tris, and zinc. In the absence of exogenous metals, this alpha-amylase bound 1 and 4 molar eq of zinc and calcium, respectively. The structure reveals a novel, activating, two-metal (Ca,Zn)-binding site and a second inhibitory zinc-binding site that is found in the -1 sugar-binding pocket within the active site. The data resolve the apparent paradox between the zinc requirement for catalytic activity and its strong inhibitory effect when added in molar excess. They provide a rationale as to why this alpha-amylase, in contrast to commercially available alpha-amylases, does not require the addition of metal ions for full catalytic activity, suggesting it as an ideal target to maximize the efficiency of industrial processes like liquefaction of starch.

PubMed: 12482867
DOI: 10.1074/jbc.M211339200

実験手法

X-RAY DIFFRACTION (2.2 Å)