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Crystal structure and biological implications of a glycoside hydrolase family 55 β-1,3-glucanase from Chaetomium thermophilum
Tekijät: Anastassios C. Papageorgiou, Jinyin Chen, Duochuan Li
Toimittaja: 2017/05/10 0
Kustantaja: ELSEVIER SCIENCE BV
Julkaisuvuosi: 2017
Journal: BBA - Proteins and Proteomics
Vuosikerta: 1865
Numero: 8
Aloitussivu: 1030
Lopetussivu: 1038
Sivujen määrä: 9
ISSN: 1570-9639
eISSN: 0006-3002
DOI: https://doi.org/10.1016/j.bbapap.2017.05.002
Tiivistelmä
Crystal structures of a beta-1,3-glucanase from the thermophilic fungus Chaetomium thermophilum were determined at 1.20 and 1.42A resolution in the free and glucose-bound form, respectively. This is the third structure of a family 55glycoside hydrolase (GH55) member and the second from a fungus. Based oncomparative structural studies and site-directed mutagenesis, Glu654 is proposedas the catalytic acid residue. The substrate binding cleft exhibits restrictedaccess on one side, rendering the enzyme as an exo-beta-1,3-glucanase asconfirmed also by thin layer chromatography experiments. A lack of stackinginteractions was found at the substrate binding cleft, suggesting thatinteractions at positions -1, +1 and +2 are sufficient to orientate thesubstrate. A binding pocket was identified that could explain binding of branchedlaminarin and accumulation of laminaritriose.CI - Copyright (c) 2017 Elsevier B.V. All rights reserved.
Crystal structures of a beta-1,3-glucanase from the thermophilic fungus Chaetomium thermophilum were determined at 1.20 and 1.42A resolution in the free and glucose-bound form, respectively. This is the third structure of a family 55glycoside hydrolase (GH55) member and the second from a fungus. Based oncomparative structural studies and site-directed mutagenesis, Glu654 is proposedas the catalytic acid residue. The substrate binding cleft exhibits restrictedaccess on one side, rendering the enzyme as an exo-beta-1,3-glucanase asconfirmed also by thin layer chromatography experiments. A lack of stackinginteractions was found at the substrate binding cleft, suggesting thatinteractions at positions -1, +1 and +2 are sufficient to orientate thesubstrate. A binding pocket was identified that could explain binding of branchedlaminarin and accumulation of laminaritriose.CI - Copyright (c) 2017 Elsevier B.V. All rights reserved.
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