Protein O -Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution.

Autor: Lira-Navarrete E; Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, 50018 Zaragoza, Spain., Pallarés MC; Instituto de Nanociencia y Materiales de Aragón (INMA), CSIC-Universidad de Zaragoza, 50009 Zaragoza, Spain.; Laboratorio de Microscopías Avanzadas (LMA), Universidad de Zaragoza, 50018 Zaragoza, Spain., Castello F; Departamento de Fisicoquímica, Facultad de Farmacia, Universidad de Granada, 18071 Granada, Spain., Ruedas-Rama MJ; Departamento de Fisicoquímica, Facultad de Farmacia, Universidad de Granada, 18071 Granada, Spain., Orte A; Departamento de Fisicoquímica, Facultad de Farmacia, Universidad de Granada, 18071 Granada, Spain., Lostao A; Instituto de Nanociencia y Materiales de Aragón (INMA), CSIC-Universidad de Zaragoza, 50009 Zaragoza, Spain.; Laboratorio de Microscopías Avanzadas (LMA), Universidad de Zaragoza, 50018 Zaragoza, Spain.; Fundación ARAID, 50018 Zaragoza, Spain., Hurtado-Guerrero R; Institute of Biocomputation and Physics of Complex Systems (BIFI), University of Zaragoza, 50018 Zaragoza, Spain.; Fundación ARAID, 50018 Zaragoza, Spain.; Laboratorio de Microscopías Avanzadas (LMA), Universidad de Zaragoza, 50018 Zaragoza, Spain.; Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, School of Dentistry, University of Copenhagen, 2200 Copenhagen, Denmark.
Jazyk: angličtina
Zdroj: Molecules (Basel, Switzerland) [Molecules] 2021 Apr 07; Vol. 26 (8). Date of Electronic Publication: 2021 Apr 07.
DOI: 10.3390/molecules26082105
Abstrakt: 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 ( Ce PoFUT1) 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 Ce PoFUT1 dynamics, which might play a role during its catalytic cycle.
Databáze: MEDLINE
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