Cryo-EM structure of the human GS-GN complex in the inhibited state
Ontology highlight
ABSTRACT:
SUBMITTER: Elton Zeqiraj
PROVIDER: EMPIAR-11139 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Mechanism of glycogen synthase inactivation and interaction with glycogenin.
Marr Laura L Biswas Dipsikha D Daly Leonard A LA Browning Christopher C Vial Sarah C M SCM Maskell Daniel P DP Hudson Catherine C Bertrand Jay A JA Pollard John J Ranson Neil A NA Khatter Heena H Eyers Claire E CE Sakamoto Kei K Zeqiraj Elton E
Nature communications 20220611 1
Glycogen is the major glucose reserve in eukaryotes, and defects in glycogen metabolism and structure lead to disease. Glycogenesis involves interaction of glycogenin (GN) with glycogen synthase (GS), where GS is activated by glucose-6-phosphate (G6P) and inactivated by phosphorylation. We describe the 2.6 Å resolution cryo-EM structure of phosphorylated human GS revealing an autoinhibited GS tetramer flanked by two GN dimers. Phosphorylated N- and C-termini from two GS protomers converge near t ...[more]
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