› 4qsh

X-ray diffraction
2.51Å resolution

Crystal Structure of L. monocytogenes Pyruvate Carboxylase in complex with Cyclic-di-AMP

Released:
DOI: 10.2210/pdb4qsh/pdb
PDB 4qsh coloured by chain and viewed from the front.
PDB 4qsh coloured by chain and viewed from the side.
PDB 4qsh coloured by chain and viewed from the top.
Source organism: Listeria monocytogenes
Primary publication:
The Cyclic Dinucleotide c-di-AMP Is an Allosteric Regulator of Metabolic Enzyme Function.
Sureka K, Choi PH, Precit M, Delince M, Pensinger DA, Huynh TN, Jurado AR, Goo YA, Sadilek M, Iavarone AT, Sauer JD, Tong L, Woodward JJ
Cell 158 1389-401 (2014)
PMID: 25215494

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate carboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 1148 amino acids
Theoretical weight: 128.53 KDa
Source organism: Listeria monocytogenes
Expression system: Escherichia coli
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand FLC 4 x FLC
Ligand MN 4 x MN
Ligand 2BA 3 x 2BA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 96.778Å b: 153.296Å c: 221.24Å
α: 90° β: 101.58° γ: 90°
R-values:
R R work R free
0.196 0.195 0.233
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Chemoproteomic Analysis of Microbiota Metabolite-Protein Targets and Mechanisms.
Zhao et al. (2022)
24 more

6 mentions without citation

Cyclic di-AMP, a second messenger of primary importance: tertiary structures and binding mechanisms.
He et al. (2020)
5 more