000151645 001__ 151645
000151645 005__ 20250319155217.0
000151645 0247_ $$2doi$$a10.3390/molecules26082105
000151645 0248_ $$2sideral$$a126644
000151645 037__ $$aART-2021-126644
000151645 041__ $$aeng
000151645 100__ $$aLira-Navarrete E.$$uUniversidad de Zaragoza
000151645 245__ $$aProtein o-fucosyltransferase 1 undergoes interdomain flexibility in solution
000151645 260__ $$c2021
000151645 5060_ $$aAccess copy available to the general public$$fUnrestricted
000151645 5203_ $$aProtein O-fucosyltransferase 1 (PoFUT1) is a GT-B fold enzyme that fucosylates proteins containing EGF-like repeats. GT-B glycosyltransferases have shown a remarkable grade of plasticity adopting closed and open conformations as a way of tuning their catalytic cycle, a feature that has not been observed for PoFUT1. Here, we analyzed Caenorhabditis elegans PoFUT1 (CePoFUT1) conformational behavior in solution by atomic force microscopy (AFM) and single-molecule fluorescence resonance energy transfer (SMF-FRET). Our results show that this enzyme is very flexible and adopts mainly compact conformations and to a lesser extend a highly dynamic population that oscillates between compact and highly extended conformations. Overall, our experiments illustrate the inherent complexity of CePoFUT1 dynamics, which might play a role during its catalytic cycle.
000151645 536__ $$9info:eu-repo/grantAgreement/ES/DGA-FEDER/E35-20R$$9info:eu-repo/grantAgreement/ES/DGA/LMP58-18$$9info:eu-repo/grantAgreement/ES/MEC/BFU2016-75633-P$$9info:eu-repo/grantAgreement/ES/MEC/CTQ2013-44367-C2-2-P$$9info:eu-repo/grantAgreement/ES/MEC/PID2019-105451GB-I00$$9info:eu-repo/grantAgreement/ES/MICINN/IJCI-2017-32874
000151645 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000151645 590__ $$a4.927$$b2021
000151645 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b114 / 297 = 0.384$$c2021$$dQ2$$eT2
000151645 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b65 / 179 = 0.363$$c2021$$dQ2$$eT2
000151645 592__ $$a0.705$$b2021
000151645 593__ $$aAnalytical Chemistry$$c2021$$dQ1
000151645 593__ $$aDrug Discovery$$c2021$$dQ1
000151645 593__ $$aPharmaceutical Science$$c2021$$dQ1
000151645 593__ $$aMolecular Medicine$$c2021$$dQ1
000151645 593__ $$aOrganic Chemistry$$c2021$$dQ1
000151645 593__ $$aMedicine (miscellaneous)$$c2021$$dQ1
000151645 594__ $$a5.9$$b2021
000151645 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000151645 700__ $$aPallarés M.C.
000151645 700__ $$aCastello F.
000151645 700__ $$aRuedas-Rama M.J.
000151645 700__ $$aOrte A.
000151645 700__ $$0(orcid)0000-0001-7460-5916$$aGracia Lostao A.
000151645 700__ $$0(orcid)0000-0002-3122-9401$$aHurtado-Guerrero R.
000151645 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000151645 773__ $$g26, 8 (2021), 2105 [14 pp.]$$pMolecules (Basel, Online)$$tMolecules$$x1420-3049
000151645 8564_ $$s3532770$$uhttps://zaguan.unizar.es/record/151645/files/texto_completo.pdf$$yVersión publicada
000151645 8564_ $$s2769142$$uhttps://zaguan.unizar.es/record/151645/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000151645 909CO $$ooai:zaguan.unizar.es:151645$$particulos$$pdriver
000151645 951__ $$a2025-03-19-14:19:57
000151645 980__ $$aARTICLE