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

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) s...

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Détails bibliographiques
Auteurs principaux:	Modenutti, CP, Blanco Capurro, JI, Ibba, R, Alonzi, DS, Song, MN, Vasiljević, S, Kumar, A, Chandran, AV, Tax, G, Marti, L, Hill, JC, Lia, A, Hensen, M, Waksman, T, Rushton, J, Rubichi, S, Santino, A, Martí, MA, Zitzmann, N, Roversi, P
Format:	Journal article
Langue:	English
Publié:	Cell Press 2020

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

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