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3 Å resolution single particle reconstruction of glucosyltransferase ALG6 in nanodisc

ABSTRACT:

SUBMITTER: Kaspar Locher

PROVIDER: EMPIAR-10429 | biostudies-other |

REPOSITORIES: biostudies-other

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Structure and mechanism of the ER-based glucosyltransferase ALG6.

Bloch Joël S JS Pesciullesi Giorgio G Boilevin Jérémy J Nosol Kamil K Irobalieva Rossitza N RN Darbre Tamis T Aebi Markus M Kossiakoff Anthony A AA Reymond Jean-Louis JL Locher Kaspar P KP

Nature 20200226 7799

In eukaryotic protein N-glycosylation, a series of glycosyltransferases catalyse the biosynthesis of a dolichylpyrophosphate-linked oligosaccharide before its transfer onto acceptor proteins<sup>1</sup>. The final seven steps occur in the lumen of the endoplasmic reticulum (ER) and require dolichylphosphate-activated mannose and glucose as donor substrates<sup>2</sup>. The responsible enzymes-ALG3, ALG9, ALG12, ALG6, ALG8 and ALG10-are glycosyltransferases of the C-superfamily (GT-Cs), which are ...[more]

PMID: 32103179

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