@misc{10481/67929,
year = {2021},
url = {http://hdl.handle.net/10481/67929},
abstract = {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.},
organization = {ARAID: MEC (CTQ2013-44367-C2-2-P, BFU2016-75633-P and PID2019-105451GBI00 to RH-G, CTQ2017-85658-R and CTQ2014-56370-R to AO)},
organization = {Gobierno de Aragón (E35_R20 and
LMP58_18)},
organization = {FEDER (2014-2020) funds for ‘Building Europe from Aragón’},
organization = {Juan de la Cierva fellowship IJCI-2017-32874},
publisher = {MDPI},
keywords = {Glycosyltransferases},
keywords = {O-fucosylation},
keywords = {Protein dynamics},
keywords = {Atomic force microscopy},
keywords = {Singlemolecule methods},
title = {Protein O-Fucosyltransferase 1 Undergoes Interdomain Flexibility in Solution},
doi = {10.3390/molecules26082105},
author = {Lira Navarrete, Erandi and Castello, Fabio and Ruedas Rama, María José and Orte Gutiérrez, Ángel},
}