4UZU

Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution

Summary for 4UZU

• Entry DOI: 10.2210/pdb4uzu/pdb
• Descriptor: ALPHA-AMYLASE, GLYCINE, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: hydrolase
• Biological source: GEOBACILLUS STEAROTHERMOPHILUS
• Total number of polymer chains: 1
• Total formula weight: 59042.42

Authors

Offen, W.A.,Anderson, C.,Borchert, T.V.,Wilson, K.S.,Davies, G.J. (deposition date: 2014-09-09, release date: 2015-01-14, Last modification date: 2024-01-10)

Primary citation

Offen, W.A.,Viksoe-Nielsen, A.,Borchert, T.V.,Wilson, K.S.,Davies, G.J.
Three-Dimensional Structure of a Variant `Termamyl-Like' Geobacillus Stearothermophilus Alpha-Amylase at 1.9 A Resolution
Acta Crystallogr.,Sect.F, 71:66-, 2015

PubMed 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 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 1.9 Å 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 3 Å in some regions, reflecting both the mutations and differing crystal-packing environments.

PubMed: 25615972
DOI: 10.1107/S2053230X14026508

Experimental method

X-RAY DIFFRACTION (1.9 Å)