Three-dimensional structure of a variant 'Termamyl-like' Geobacillus stearothermophilus α-amylase at 1.9Å resolution

Wendy A. Offen, Anders Viksoe-Nielsen, Torben V. Borchert, Keith S. Wilson, Gideon J. Davies*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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 α-amylases and then exo-acting α-glucosidases (glucoamylases) to yield glucose, which is subsequently processed. A key enzymatic player in this pipeline is the 'Termamyl' class of bacterial α-amylases and designed/evolved variants thereof. Here, the three-dimensional structure of one such Termamyl α-amylase variant based upon the parent Geobacillus stearothermophilus α-amylase is presented. The structure has been solved at 1.9Å resolution, revealing the classical three-domain fold stabilized by Ca2+ and a Ca2+-Na+-Ca2+ triad. As expected, the structure is similar to the G. stearothermophilus α-amylase but with main-chain deviations of up to 3Å in some regions, reflecting both the mutations and differing crystal-packing environments.

Original languageEnglish
Pages (from-to)66-70
Number of pages5
JournalActa Crystallographica Section F:Structural Biology Communications
Issue number1
Publication statusPublished - Jan 2015


  • Amylase
  • Geobacillus stearothermophilus
  • Termamyl

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