› 1xkv

X-ray diffraction
2.2Å resolution

Crystal Structure Of ATP-Dependent Phosphoenolpyruvate Carboxykinase From Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1xkv/pdb
PDB entry 1xkv coloured by chain, front view.
PDB entry 1xkv coloured by chain, side view.
PDB entry 1xkv coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Structure of ATP-dependent phosphoenolpyruvate carboxykinase from Thermus thermophilus HB8 showing the structural basis of induced fit and thermostability.
Sugahara M, Ohshima N, Ukita Y, Sugahara M, Kunishima N
Acta Crystallogr D Biol Crystallogr 61 1500-7 (2005)
PMID: 16239727

Function and Biology Details

Reaction catalysed: 
ATP + oxaloacetate = ADP + phosphoenolpyruvate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178181 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxykinase (ATP) Chains: A, B
Molecule details ›
Chains: A, B
Length: 529 amino acids
Theoretical weight: 59.39 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SLL5 (Residues: 1-529; Coverage: 100%)
Gene names: TTHA0278, pckA, tthHB8IM
Sequence domains: Phosphoenolpyruvate carboxykinase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CA 2 x CA
Ligand PO4 6 x PO4
Ligand ATP 1 x ATP
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 65.067Å b: 130.548Å c: 174.195Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.219
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism.
Bagautdinov et al. (2007)
5 more

2 mentions without citation

Short and simple sequences favored the emergence of N-helix phospho-ligand binding sites in the first enzymes.
Longo et al. (2020)
1 more