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Structure paper

TitleMolecular basis for the regulation of human glycogen synthase by phosphorylation and glucose-6-phosphate.
Journal, issue, pagesNat Struct Mol Biol, Vol. 29, Issue 7, Page 628-638, Year 2022
Publish dateJul 14, 2022
AuthorsThomas J McCorvie / Paula M Loria / Meihua Tu / Seungil Han / Leela Shrestha / D Sean Froese / Igor M Ferreira / Allison P Berg / Wyatt W Yue /
PubMed AbstractGlycogen synthase (GYS1) is the central enzyme in muscle glycogen biosynthesis. GYS1 activity is inhibited by phosphorylation of its amino (N) and carboxyl (C) termini, which is relieved by ...Glycogen synthase (GYS1) is the central enzyme in muscle glycogen biosynthesis. GYS1 activity is inhibited by phosphorylation of its amino (N) and carboxyl (C) termini, which is relieved by allosteric activation of glucose-6-phosphate (Glc6P). We present cryo-EM structures at 3.0-4.0 Å resolution of phosphorylated human GYS1, in complex with a minimal interacting region of glycogenin, in the inhibited, activated and catalytically competent states. Phosphorylations of specific terminal residues are sensed by different arginine clusters, locking the GYS1 tetramer in an inhibited state via intersubunit interactions. The Glc6P activator promotes conformational change by disrupting these interactions and increases the flexibility of GYS1, such that it is poised to adopt a catalytically competent state when the sugar donor UDP-glucose (UDP-glc) binds. We also identify an inhibited-like conformation that has not transitioned into the activated state, in which the locking interaction of phosphorylation with the arginine cluster impedes subsequent conformational changes due to Glc6P binding. Our results address longstanding questions regarding the mechanism of human GYS1 regulation.
External linksNat Struct Mol Biol / PubMed:35835870 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 4.0 Å
Structure data

13743

7q0b

EMDB-13743, PDB-7q0b:
Human GYS1-GYG1 complex inhibited state
Method: EM (single particle) / Resolution: 3.0 Å

13751

7q0s

EMDB-13751, PDB-7q0s:
Human GYS1-GYG1 complex inhibited-like state bound to glucose-6-phosphate
Method: EM (single particle) / Resolution: 4.0 Å

13752

7q12

EMDB-13752, PDB-7q12:
Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate
Method: EM (single particle) / Resolution: 3.7 Å

13753

7q13

EMDB-13753, PDB-7q13:
Human GYS1-GYG1 complex activated state bound to glucose-6-phosphate, uridine diphosphate, and glucose
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-G6P:
6-O-phosphono-alpha-D-glucopyranose

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM / Uridine diphosphate

ChemComp-GLC:
alpha-D-glucopyranose / Glucose

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Glycogen / Complex / Phosphorylation

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