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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التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	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
التنسيق:	Journal article
اللغة:	English
منشور في:	Cell Press 2020

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

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