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Title: Small-angle scattering study of Aspergillus awamori glycoprotein glucoamylase

Glucoamylase from fungus Aspergillus awamori is glycoside hydrolase that catalyzes the hydrolysis of α-1,4- and α-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 Å.
Authors:
;  [1] ;  [2] ; ; ; ;  [1]
  1. National Research Center “Kurchatov Institute”, Konstantinov Petersburg Nuclear Physics Institute (Russian Federation)
  2. Joint Institute for Nuclear Research (Russian Federation)
Publication Date:
OSTI Identifier:
22471909
Resource Type:
Journal Article
Resource Relation:
Journal Name: Crystallography Reports; Journal Volume: 61; Journal Issue: 1; Other Information: Copyright (c) 2016 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; ASPERGILLUS; CHEMICAL BONDS; ENZYMES; GLUCOSE; GLYCOPROTEINS; GLYCOSIDES; HYDROLYSIS; MONOMERS; NEUTRON DIFFRACTION; POLYMERS; POLYPEPTIDES; SMALL ANGLE SCATTERING; STARCH