› 1ult

X-ray diffraction
2.55Å resolution

Crystal structure of tt0168 from Thermus thermophilus HB8

Released:
DOI: 10.2210/pdb1ult/pdb
PDB entry 1ult coloured by chain, front view.
PDB entry 1ult coloured by chain, side view.
PDB entry 1ult coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer.
Hisanaga Y, Ago H, Nakagawa N, Hamada K, Ida K, Yamamoto M, Hori T, Arii Y, Sugahara M, Kuramitsu S, Yokoyama S, Miyano M
J Biol Chem 279 31717-26 (2004)
PMID: 15145952

Function and Biology Details

Reaction catalysed: 
ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178101 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Long-chain-fatty-acid--CoA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 541 amino acids
Theoretical weight: 59.65 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SKN9 (Residues: 1-541; Coverage: 100%)
Gene name: TTHA0604
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 55.952Å b: 124.687Å c: 212.471Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.239
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Carnitine transport and fatty acid oxidation.
Longo et al. (2016)
21 more

9 mentions without citation

Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase.
Gulick AM. (2009)
8 more