Small-angle scattering study of Aspergillus awamori glycoprotein glucoamylase. Schmidt, A., Shvetsov, A., Kuklin, A., Lebedev, D., Surzhik, M., Sergeev, V., & Isaev-Ivanov, V. Crystallography Reports, 61(1):149-152, 2016. cited By 1![Small-angle scattering study of Aspergillus awamori glycoprotein glucoamylase [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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. © 2016, Pleiades Publishing, Inc.
@ARTICLE{Schmidt2016149,
author={Schmidt, A.E. and Shvetsov, A.V. and Kuklin, A.I. and Lebedev, D.V. and Surzhik, M.A. and Sergeev, V.R. and Isaev-Ivanov, V.V.},
title={Small-angle scattering study of Aspergillus awamori glycoprotein glucoamylase},
journal={Crystallography Reports},
year={2016},
volume={61},
number={1},
pages={149-152},
doi={10.1134/S1063774516010223},
note={cited By 1},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-84955578899&doi=10.1134%2fS1063774516010223&partnerID=40&md5=ec97b1e534a5b01b73f260682af7ee41},
affiliation={Konstantinov Petersburg Nuclear Physics Institute, National Research Center “Kurchatov Institute”, Orlova Roscha, Gatchina, Leningrad oblast, 188300, Russian Federation; Joint Institute for Nuclear Research, ul. Joliot-Curie 6, Dubna, Moscow region, 141980, Russian Federation; Research-Educational Centre “Bionanophysics”, Moscow Institute of Physics and Technology (State University), Institutskii per. 9, Dolgoprudny, Moscow region, 141700, Russian Federation; St. Petersburg State Polytechnical University, Politekhnicheskaya ul. 29, St. Petersburg, 195251, Russian Federation},
abstract={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. © 2016, Pleiades Publishing, Inc.},
funding_details={Российский Фонд Фундаментальных Исследований (РФФИ)14-24-01103 ofi-m},
}
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Joliot-Curie 6, Dubna, Moscow region, 141980, Russian Federation; Research-Educational Centre “Bionanophysics”, Moscow Institute of Physics and Technology (State University), Institutskii per. 9, Dolgoprudny, Moscow region, 141700, Russian Federation; St. Petersburg State Polytechnical University, Politekhnicheskaya ul. 29, St. Petersburg, 195251, Russian Federation},\r\nabstract={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. 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