The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences

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Standard

The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences. / Rivas, Matilde De Las; Lira-Navarrete, Erandi; Daniel, Earnest James Paul; Companõn, Ismael; Coelho, Helena; Diniz, Ana; Jiménez-Barbero, Jesús; Peregrina, Jesús M.; Clausen, Henrik; Corzana, Francisco; Marcelo, Filipa; Jiménez-Osés, Gonzalo; Gerken, Thomas A.; Hurtado-Guerrero, Ramon.

I: Nature Communications, Bind 8, Nr. 1, 1959, 12.2017.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Rivas, MDL, Lira-Navarrete, E, Daniel, EJP, Companõn, I, Coelho, H, Diniz, A, Jiménez-Barbero, J, Peregrina, JM, Clausen, H, Corzana, F, Marcelo, F, Jiménez-Osés, G, Gerken, TA & Hurtado-Guerrero, R 2017, 'The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences', Nature Communications, bind 8, nr. 1, 1959. https://doi.org/10.1038/s41467-017-02006-0

APA

Rivas, M. D. L., Lira-Navarrete, E., Daniel, E. J. P., Companõn, I., Coelho, H., Diniz, A., Jiménez-Barbero, J., Peregrina, J. M., Clausen, H., Corzana, F., Marcelo, F., Jiménez-Osés, G., Gerken, T. A., & Hurtado-Guerrero, R. (2017). The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences. Nature Communications, 8(1), [1959]. https://doi.org/10.1038/s41467-017-02006-0

Vancouver

Rivas MDL, Lira-Navarrete E, Daniel EJP, Companõn I, Coelho H, Diniz A o.a. The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences. Nature Communications. 2017 dec;8(1). 1959. https://doi.org/10.1038/s41467-017-02006-0

Author

Rivas, Matilde De Las ; Lira-Navarrete, Erandi ; Daniel, Earnest James Paul ; Companõn, Ismael ; Coelho, Helena ; Diniz, Ana ; Jiménez-Barbero, Jesús ; Peregrina, Jesús M. ; Clausen, Henrik ; Corzana, Francisco ; Marcelo, Filipa ; Jiménez-Osés, Gonzalo ; Gerken, Thomas A. ; Hurtado-Guerrero, Ramon. / The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences. I: Nature Communications. 2017 ; Bind 8, Nr. 1.

Bibtex

@article{c404aa59b43d415985073498c2852a0e,
title = "The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences",
abstract = "The polypeptide GalNAc-transferases (GalNAc-Ts), that initiate mucin-type O-glycosylation, consist of a catalytic and a lectin domain connected by a flexible linker. In addition to recognizing polypeptide sequence, the GalNAc-Ts exhibit unique long-range N- A nd/or C-terminal prior glycosylation (GalNAc-O-Ser/Thr) preferences modulated by the lectin domain. Here we report studies on GalNAc-T4 that reveal the origins of its unique N-terminal long-range glycopeptide specificity, which is the opposite of GalNAc-T2. The GalNAc-T4 structure bound to a monoglycopeptide shows that the GalNAc-binding site of its lectin domain is rotated relative to the homologous GalNAc-T2 structure, explaining their different long-range preferences. Kinetics and molecular dynamics simulations on several GalNAc-T2 flexible linker constructs show altered remote prior glycosylation preferences, confirming that the flexible linker dictates the rotation of the lectin domain, thus modulating the GalNAc-Ts' long-range preferences. This work for the first time provides the structural basis for the different remote prior glycosylation preferences of the GalNAc-Ts.",
author = "Rivas, {Matilde De Las} and Erandi Lira-Navarrete and Daniel, {Earnest James Paul} and Ismael Compan{\~o}n and Helena Coelho and Ana Diniz and Jes{\'u}s Jim{\'e}nez-Barbero and Peregrina, {Jes{\'u}s M.} and Henrik Clausen and Francisco Corzana and Filipa Marcelo and Gonzalo Jim{\'e}nez-Os{\'e}s and Gerken, {Thomas A.} and Ramon Hurtado-Guerrero",
year = "2017",
month = dec,
doi = "10.1038/s41467-017-02006-0",
language = "English",
volume = "8",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences

AU - Rivas, Matilde De Las

AU - Lira-Navarrete, Erandi

AU - Daniel, Earnest James Paul

AU - Companõn, Ismael

AU - Coelho, Helena

AU - Diniz, Ana

AU - Jiménez-Barbero, Jesús

AU - Peregrina, Jesús M.

AU - Clausen, Henrik

AU - Corzana, Francisco

AU - Marcelo, Filipa

AU - Jiménez-Osés, Gonzalo

AU - Gerken, Thomas A.

AU - Hurtado-Guerrero, Ramon

PY - 2017/12

Y1 - 2017/12

N2 - The polypeptide GalNAc-transferases (GalNAc-Ts), that initiate mucin-type O-glycosylation, consist of a catalytic and a lectin domain connected by a flexible linker. In addition to recognizing polypeptide sequence, the GalNAc-Ts exhibit unique long-range N- A nd/or C-terminal prior glycosylation (GalNAc-O-Ser/Thr) preferences modulated by the lectin domain. Here we report studies on GalNAc-T4 that reveal the origins of its unique N-terminal long-range glycopeptide specificity, which is the opposite of GalNAc-T2. The GalNAc-T4 structure bound to a monoglycopeptide shows that the GalNAc-binding site of its lectin domain is rotated relative to the homologous GalNAc-T2 structure, explaining their different long-range preferences. Kinetics and molecular dynamics simulations on several GalNAc-T2 flexible linker constructs show altered remote prior glycosylation preferences, confirming that the flexible linker dictates the rotation of the lectin domain, thus modulating the GalNAc-Ts' long-range preferences. This work for the first time provides the structural basis for the different remote prior glycosylation preferences of the GalNAc-Ts.

AB - The polypeptide GalNAc-transferases (GalNAc-Ts), that initiate mucin-type O-glycosylation, consist of a catalytic and a lectin domain connected by a flexible linker. In addition to recognizing polypeptide sequence, the GalNAc-Ts exhibit unique long-range N- A nd/or C-terminal prior glycosylation (GalNAc-O-Ser/Thr) preferences modulated by the lectin domain. Here we report studies on GalNAc-T4 that reveal the origins of its unique N-terminal long-range glycopeptide specificity, which is the opposite of GalNAc-T2. The GalNAc-T4 structure bound to a monoglycopeptide shows that the GalNAc-binding site of its lectin domain is rotated relative to the homologous GalNAc-T2 structure, explaining their different long-range preferences. Kinetics and molecular dynamics simulations on several GalNAc-T2 flexible linker constructs show altered remote prior glycosylation preferences, confirming that the flexible linker dictates the rotation of the lectin domain, thus modulating the GalNAc-Ts' long-range preferences. This work for the first time provides the structural basis for the different remote prior glycosylation preferences of the GalNAc-Ts.

U2 - 10.1038/s41467-017-02006-0

DO - 10.1038/s41467-017-02006-0

M3 - Journal article

C2 - 29208955

AN - SCOPUS:85037122538

VL - 8

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 1959

ER -

ID: 187048940