1MXD: Structure Of A (Ca,Zn)-Dependent Alpha-Amylase From The Hyperthermophilic Archaeon Pyrococcus Woesei

Citation:
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.
PDB ID: 1MXDDownload
MMDB ID: 23406
PDB Deposition Date: 2002/10/2
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1MXD: monomeric; determined by author
Molecular Components in 1MXD
Label Count Molecule
Protein (1 molecule)
1
Alpha Amylase
Molecule annotation
Chemicals (13 molecules)
1
4
2
1
3
6
4
1
5
1
* Click molecule labels to explore molecular sequence information.

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