› 6shq

Electron Microscopy
3.2Å resolution

Escherichia coli AGPase in complex with AMP. Symmetry C2

Released:
DOI: 10.2210/pdb6shq/pdb
PDB entry 6shq coloured by chain, front view.
PDB entry 6shq coloured by chain, side view.
PDB entry 6shq coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The allosteric control mechanism of bacterial glycogen biosynthesis disclosed by cryoEM.
Cifuente JO, Comino N, D'Angelo C, Marina A, Gil-Carton D, Albesa-Jové D, Guerin ME
OpenAccess logo Curr Res Struct Biol 2 89-103 (2020)
PMID: 34235472
Related structures: EMD-10203

Function and Biology Details

Reaction catalysed: 
ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141432 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-1-phosphate adenylyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 431 amino acids
Theoretical weight: 48.76 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6V1 (Residues: 1-431; Coverage: 100%)
Gene names: JW3393, b3430, glgC
Sequence domains: Nucleotidyl transferase

Ligands and Environments

1 bound ligand:
Ligand AMP 4 x AMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.2Å
Relevant EMDB volumes: EMD-10203
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biomedical Applications of Bacteria-Derived Polymers.
Hinchliffe et al. (2021)
1 more

1 mention without citation

The allosteric control mechanism of bacterial glycogen biosynthesis disclosed by cryoEM.
Cifuente et al. (2020)