Protein o-fucosyltransferase 1 undergoes interdomain flexibility in solution

Lira-Navarrete E. (Universidad de Zaragoza) ; Pallarés M.C. ; Castello F. ; Ruedas-Rama M.J. ; Orte A. ; Gracia Lostao A. ; Hurtado-Guerrero R.

Resumen: 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.

Idioma: Inglés

DOI: 10.3390/molecules26082105

Año: 2021

Publicado en: Molecules 26, 8 (2021), 2105 [14 pp.]
ISSN: 1420-3049

Factor impacto JCR: 4.927 (2021)

Categ. JCR: CHEMISTRY, MULTIDISCIPLINARY rank: 65 / 179 = 0.363 (2021) - Q2 - T2
Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 114 / 297 = 0.384 (2021) - Q2 - T2

Factor impacto CITESCORE: 5.9 - Pharmacology, Toxicology and Pharmaceutics (Q2) - Biochemistry, Genetics and Molecular Biology (Q2)

Factor impacto SCIMAGO: 0.705 - Analytical Chemistry (Q1) - Drug Discovery (Q1) - Pharmaceutical Science (Q1) - Molecular Medicine (Q1) - Organic Chemistry (Q1) - Medicine (miscellaneous) (Q1)

Financiación: info:eu-repo/grantAgreement/ES/DGA-FEDER/E35-20R
Financiación: info:eu-repo/grantAgreement/ES/DGA/LMP58-18
Financiación: info:eu-repo/grantAgreement/ES/MEC/BFU2016-75633-P
Financiación: info:eu-repo/grantAgreement/ES/MEC/CTQ2013-44367-C2-2-P
Financiación: info:eu-repo/grantAgreement/ES/MEC/PID2019-105451GB-I00
Financiación: info:eu-repo/grantAgreement/ES/MICINN/IJCI-2017-32874

Tipo y forma: Article (Published version)

Área (Departamento): Área Bioquímica y Biolog.Mole. (Dpto. Bioq.Biolog.Mol. Celular)