doi:10.3390/molecules26082105engLira-Navarrete E.Pallarés M.C.Castello F.Ruedas-Rama M.J.Orte A.Gracia Lostao A.Hurtado-Guerrero R.Protein o-fucosyltransferase 1 undergoes interdomain flexibility in solutionART-2021-126644Protein 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.2021http://zaguan.unizar.es/record/15164510.3390/molecules26082105http://zaguan.unizar.es/record/151645oai:zaguan.unizar.es:151645info:eu-repo/grantAgreement/ES/DGA-FEDER/E35-20Rinfo:eu-repo/grantAgreement/ES/DGA/LMP58-18info:eu-repo/grantAgreement/ES/MEC/BFU2016-75633-Pinfo:eu-repo/grantAgreement/ES/MEC/CTQ2013-44367-C2-2-Pinfo:eu-repo/grantAgreement/ES/MEC/PID2019-105451GB-I00info:eu-repo/grantAgreement/ES/MICINN/IJCI-2017-32874Molecules 26, 8 (2021), 2105 [14 pp.]byhttps://creativecommons.org/licenses/by/4.0/deed.esinfo:eu-repo/semantics/openAccess