Journal
CRYSTALLOGRAPHY REPORTS
Volume 61, Issue 1, Pages 149-152Publisher
MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S1063774516010223
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- Russian Foundation for Basic Research [14-24-01103 ofi-m]
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Glucoamylase from fungus Aspergillus awamori is glycoside hydrolase that catalyzes the hydrolysis of alpha-1,4- and alpha-1,6-glucosidic bonds in glucose polymers and oligomers. This glycoprotein consists of a catalytic domain and a starch-binding domain connected by an O-glycosylated polypeptide chain. The conformation of the linker, the relative arrangement of the domains, and the structure of the full-length enzyme are unknown. The structure of the recombinant glucoamylase GA1 was studied by molecular modelling and small-angle neutron scattering (SANS) methods. The experimental SANS data provide evidence that glucoamylase exists as a monomer in solution and contains a glycoside component, which makes a substantial contribution to the scattering. The model of full-length glucoamylase, which was calculated without taking into account the effect of glycosylation, is consistent with the experimental data and has a radius of gyration of 33.4 +/- 0.6 angstrom.
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