› 1ixe

X-ray diffraction
2.3Å resolution

Crystal structure of citrate synthase from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1ixe/pdb
PDB entry 1ixe coloured by chain, front view.
PDB entry 1ixe coloured by chain, side view.
PDB entry 1ixe coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structural comparison between the open and closed forms of citrate synthase from Thermus thermophilus HB8.
Kanamori E, Kawaguchi S, Kuramitsu S, Kouyama T, Murakami M
Biophys Physicobiol 12 47-56 (2015)
PMID: 27493854

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177967 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Citrate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 377 amino acids
Theoretical weight: 42.36 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SIM6 (Residues: 1-377; Coverage: 100%)
Gene name: TTHA1343
Sequence domains: Citrate synthase, C-terminal domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SO4 10 x SO4
Ligand COA 4 x COA
Ligand CIT 4 x CIT
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 80.01Å b: 110.63Å c: 184.382Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.217
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

A primordial and reversible TCA cycle in a facultatively chemolithoautotrophic thermophile.
Nunoura et al. (2018)
4 more

1 mention without citation

Structural comparison between the open and closed forms of citrate synthase from Thermus thermophilus HB8.
Kanamori et al. (2015)