1MWO

Crystal Structure Analysis of the Hyperthermostable Pyrocoocus woesei alpha-amylase

Summary for 1MWO

• Entry DOI: 10.2210/pdb1mwo/pdb
• Related: 1MXD 1MXG
• Descriptor: alpha amylase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: (beta/alpha)8-barrel, alpha-amylase, hydrolase
• Biological source: Pyrococcus woesei
• Total number of polymer chains: 1
• Total formula weight: 50661.21

Authors

Linden, A.,Mayans, O.,Meyer-Klaucke, W.,Antranikian, G.,Wilmanns, M. (deposition date: 2002-09-30, release date: 2003-06-10, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)