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Article

Protein O-Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution

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Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, 50018 Zaragoza, Spain
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Instituto de Nanociencia y Materiales de Aragón (INMA), CSIC-Universidad de Zaragoza, 50009 Zaragoza, Spain
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Laboratorio de Microscopías Avanzadas (LMA), Universidad de Zaragoza, 50018 Zaragoza, Spain
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Departamento de Fisicoquímica, Facultad de Farmacia, Universidad de Granada, 18071 Granada, Spain
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Fundación ARAID, 50018 Zaragoza, Spain
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Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, School of Dentistry, University of Copenhagen, 2200 Copenhagen, Denmark
*
Authors to whom correspondence should be addressed.
Academic Editors: Vassilis Tangoulis and Vladimir N. Uversky
Molecules 2021, 26(8), 2105; https://doi.org/10.3390/molecules26082105
Received: 7 February 2021 / Revised: 22 March 2021 / Accepted: 2 April 2021 / Published: 7 April 2021
(This article belongs to the Special Issue New Insights into Protein Glycosylation)
Protein O-fucosyltransferase 1 (PoFUT1) is a GT-B fold enzyme that fucosylates proteins containing EGF-like repeats. GT-B glycosyltransferases have shown a remarkable grade of plasticity adopting closed and open conformations as a way of tuning their catalytic cycle, a feature that has not been observed for PoFUT1. Here, we analyzed Caenorhabditis elegans PoFUT1 (CePoFUT1) conformational behavior in solution by atomic force microscopy (AFM) and single-molecule fluorescence resonance energy transfer (SMF-FRET). Our results show that this enzyme is very flexible and adopts mainly compact conformations and to a lesser extend a highly dynamic population that oscillates between compact and highly extended conformations. Overall, our experiments illustrate the inherent complexity of CePoFUT1 dynamics, which might play a role during its catalytic cycle. View Full-Text
Keywords: glycosyltransferases; O-fucosylation; protein dynamics; atomic force microscopy; single-molecule methods glycosyltransferases; O-fucosylation; protein dynamics; atomic force microscopy; single-molecule methods
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MDPI and ACS Style

Lira-Navarrete, E.; Pallarés, M.C.; Castello, F.; Ruedas-Rama, M.J.; Orte, A.; Lostao, A.; Hurtado-Guerrero, R. Protein O-Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution. Molecules 2021, 26, 2105. https://doi.org/10.3390/molecules26082105

AMA Style

Lira-Navarrete E, Pallarés MC, Castello F, Ruedas-Rama MJ, Orte A, Lostao A, Hurtado-Guerrero R. Protein O-Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution. Molecules. 2021; 26(8):2105. https://doi.org/10.3390/molecules26082105

Chicago/Turabian Style

Lira-Navarrete, Erandi, María C. Pallarés, Fabio Castello, Maria J. Ruedas-Rama, Angel Orte, Anabel Lostao, and Ramón Hurtado-Guerrero. 2021. "Protein O-Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution" Molecules 26, no. 8: 2105. https://doi.org/10.3390/molecules26082105

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