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Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase

Modenutti, Carlos Pablo et al · Cell Press · 2021

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Author / responsible party
Modenutti, Carlos Pablo et al
Publisher
Cell Press
Year
2021
ISSN
0969-2126
ISSN
0969-2126
Language
English

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UDP-glucose:glycoprotein glucosyltransferase (UGGT) flags misfolded glycoproteins for ER retention. We report crystal structures of full-length Chaetomium thermophilum UGGT (CtUGGT), two CtUGGT double-cysteine mutants, and its TRXL2 domain truncation (CtUGGT-ΔTRXL2). CtUGGT molecular dynamics (MD) simulations capture extended conformations and reveal clamping, bending, and twisting inter-domain movements. We name “Parodi limit” the maximum distance on the same glycoprotein between a site of misfolding and an N-linked glycan that can be reglucosylated by monomeric UGGT in vitro, in response to recognition of misfold at that site. Based on the MD simulations, we estimate the Parodi limit as around 70–80 Å. Frequency distributions of distances between glycoprotein residues and their closest N-linked glycosylation sites in glycoprotein crystal structures suggests relevance of the Parodi limit to UGGT activity in vivo. Our data support a “one-size-fits-all adjustable spanner” UGGT substrate recognition model, with an essential role for the UGGT TRXL2 domain. Fil: Modenutti, Carlos Pablo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Blanco Capurro, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina

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APA 7

Modenutti, C. P. E. A. (2021). Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase. http://hdl.handle.net/11336/210321

MLA

Modenutti, Carlos Pablo et al. "Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase." 2021. http://hdl.handle.net/11336/210321.

Chicago

Modenutti, Carlos Pablo et al. 2021. "Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase.". http://hdl.handle.net/11336/210321.

Harvard

Modenutti, C. P. E. A. 2021, Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase, Cell Press, available at: http://hdl.handle.net/11336/210321 [Accessed 8 Aug. 2026].

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Title
Clamping, bending, and twisting inter-domain motions in the misfold-recognizing portion of UDP-glucose: Glycoprotein glucosyltransferase
Author / contributors
Modenutti, Carlos Pablo et al
Publisher
Cell Press
Publication year
2021
ISSN
0969-2126
ISSN
0969-2126
Language
English

Subjects

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GLYCOPROTEIN FOLDING; GT24 DOMAIN; MISFOLD SENSING; MISFOLDING; MOLECULAR DYNAMICS; NEGATIVE-STAIN EM; PARODI LIMIT; RE-GLUCOSYLATION; UGGT; X-RAY DIFFRACTION; https://purl.org/becyt/ford/1.6; https://purl.org/becyt/ford/1
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