4UZU: Three-dimensional Structure Of A Variant `termamyl-like' Geobacillus Stearothermophilus Alpha-amylase At 1.9 A Resolution

Citation:
Abstract
The enzyme-catalysed degradation of starch is central to many industrial processes, including sugar manufacture and first-generation biofuels. Classical biotechnological platforms involve steam explosion of starch followed by the action of endo-acting glycoside hydrolases termed alpha-amylases and then exo-acting alpha-glucosidases (glucoamylases) to yield glucose, which is subsequently processed. A key enzymatic player in this pipeline is the `Termamyl' class of bacterial alpha-amylases and designed/evolved variants thereof. Here, the three-dimensional structure of one such Termamyl alpha-amylase variant based upon the parent Geobacillus stearothermophilus alpha-amylase is presented. The structure has been solved at 1.9 A resolution, revealing the classical three-domain fold stabilized by Ca(2+) and a Ca(2+)-Na(+)-Ca(2+) triad. As expected, the structure is similar to the G. stearothermophilus alpha-amylase but with main-chain deviations of up to 3 A in some regions, reflecting both the mutations and differing crystal-packing environments.
PDB ID: 4UZUDownload
MMDB ID: 126108
PDB Deposition Date: 2014/9/9
Updated in MMDB: 2015/02
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 4UZU: monomeric; determined by author and by software (PISA)
Molecular Components in 4UZU
Label Count Molecule
Protein (1 molecule)
1
Alpha-amylase
Molecule annotation
Chemicals (10 molecules)
1
2
2
3
3
2
4
3
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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