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TitleStructural and mechanistic diversity of glycogen phosphorylases from gut bacteria
Journal, issue, pagesTo Be Published
Publish dateJun 4, 2025 (structure data deposition date)
AuthorsShobu K / Takai M / Tanino H / Fukuda Y / Inoue T
External linksSearch PubMed
MethodsEM (single particle) / X-ray diffraction
Resolution2.96 - 3.55 Å
Structure data

64926

9vbl

EMDB-64926, PDB-9vbl:
Cryo-EM structure of glycogen phosphorylase from Dorea longicatena (monomer form)
Method: EM (single particle) / Resolution: 3.39 Å

64927

9vbm

EMDB-64927, PDB-9vbm:
Cryo-EM structure of glycogen phosphorylase from Dorea longicatena (dimer form)
Method: EM (single particle) / Resolution: 3.19 Å

EMDB-64931: Cryo-EM map of glycogen phosphorylase from Dorea longicatena (monomer form with extra density)
Method: EM (single particle) / Resolution: 3.3 Å

67417

20yr

EMDB-67417, PDB-20yr:
R583A mutant of glycogen phosphorylase from Segatella copri
Method: EM (single particle) / Resolution: 3.0 Å

67418

20ys

EMDB-67418, PDB-20ys:
R583A mutant of glycogen phosphorylase from Segatella copri in the presence of AMP
Method: EM (single particle) / Resolution: 2.96 Å

PDB-9ukq:
Crystal structure of glycogen phosphorylase from Escherichia coli
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

PDB-9ukr:
Crystal structure of glycogen phosphorylase from E. coli in complex with AMP
Method: X-RAY DIFFRACTION / Resolution: 3.55 Å

PDB-9v16:
Crystal structure of E. coli glycogen phosphorylase N185A/R267E mutant in complex with AMP
Method: X-RAY DIFFRACTION / Resolution: 3.45 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • dorea longicatena (bacteria)
  • segatella copri (bacteria)
  • escherichia coli k12 (bacteria)
  • escherichia coli k-12 (bacteria)
KeywordsTRANSFERASE / glycogen phosphorylase

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