Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase)

Gee, Christine L.; Holton, James M.; McPherson, Alexander

doi:10.1016/j.jbiosc.2021.02.008

Title: Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase)

Journal Article · Fri Apr 02 00:00:00 EDT 2021 · Journal of Bioscience and Bioengineering

DOI:https://doi.org/10.1016/j.jbiosc.2021.02.008· OSTI ID:1807890

^[1]; Holton, James M. ^[2];

^[3]

Univ. of California, Berkeley, CA (United States). Dept. of Molecular and Cell Biology, Howard Hughes Medical Institute
Univ. of California, San Francisco, CA (United States). Dept. of Biochemistry and Biophysics; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Univ. of California, Irvine, CA (United States). Dept. of Molecular Biology and Biochemistry

The structures of Aspergillus oryzae α-amylase were determined in a tetragonal crystal, having one molecule as asymmetric unit, and a monoclinic crystal with two molecules as asymmetric unit. Both crystal forms were obtained from trace contaminants of an old commercial lipase preparation. Structures were determined and refined to 1.65 Å and 1.43 Å resolution respectively. The latter crystal has a non-crystallographic (NCS) twofold axis within the asymmetric unit. Glycosylation at Asn197 is evident, and in the tetragonal crystal can be seen to include three, partially disordered sugar residues following the initial N-acetyl glucosamine (NAG). Superposition of the tetragonal crystal model on the α-amylases from Bacillus subtilis (PDB:1BAG), pig pancreas (PDB:3L2L), and barley (PDB:1AMY), show a high degree of coincidence, particularly for the (β/α)8-barrel domains, and especially within the active site. Using this structural agreement between amylases, we extrapolated the binding model of a six residue, limit dextrin found in pig pancreas α-amylase to the A. oryzae enzyme model, which predicts substrate interacting amino acid residues.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1807890

Journal Information:: Journal of Bioscience and Bioengineering, Vol. 131, Issue 6; ISSN 1389-1723

Publisher:: Society for Bioscience and BioengineeringCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
Glycosylation
Limit dextrin
Homology
Substrate complex
Hydration
X-ray

Title: Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase)

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