Protein O -Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution

Protein -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 obser...

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Veröffentlicht in:Molecules (Basel, Switzerland) Switzerland), 2021-04, Vol.26 (8), p.2105
Hauptverfasser: Lira-Navarrete, Erandi, Pallarés, María Carmen, Castello, Fabio, Ruedas-Rama, Maria J, Orte, Angel, Lostao, Anabel, Hurtado-Guerrero, Ramón
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Sprache:eng
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Zusammenfassung:Protein -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 PoFUT1 ( 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 PoFUT1 dynamics, which might play a role during its catalytic cycle.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules26082105