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

TY - JOUR

T1 - Three-dimensional structure of a variant 'Termamyl-like' Geobacillus stearothermophilus α-amylase at 1.9Å resolution

AU - Offen, Wendy A.

AU - Viksoe-Nielsen, Anders

AU - Borchert, Torben V.

AU - Wilson, Keith S.

AU - Davies, Gideon J.

PY - 2015/1

Y1 - 2015/1

N2 - 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.

AB - 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.

KW - Amylase

KW - Geobacillus stearothermophilus

KW - Termamyl

UR - http://www.scopus.com/inward/record.url?scp=84921745976&partnerID=8YFLogxK

U2 - 10.1107/S2053230X14026508

DO - 10.1107/S2053230X14026508

M3 - Article

AN - SCOPUS:84921745976

SN - 2053-230X

VL - 71

SP - 66

EP - 70

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

IS - 1

ER -