› 8rpk

X-ray diffraction
2.62Å resolution

AMP-forming Acetyl-CoA synthetase from Chloroflexota bacterium without bound ligand

Released:
DOI: 10.2210/pdb8rpk/pdb
PDB entry 8rpk coloured by chain, front view.
PDB entry 8rpk coloured by chain, side view.
PDB entry 8rpk coloured by chain, top view.
Source organism: Chloroflexota bacterium
Primary publication:
Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.
Qin C, Graf LG, Striska K, Janetzky M, Geist N, Specht R, Schulze S, Palm GJ, Girbardt B, Dörre B, Berndt L, Kemnitz S, Doerr M, Bornscheuer UT, Delcea M, Lammers M
Nat Commun 15 6002 (2024)
PMID: 39019872

Function and Biology Details

Reaction catalysed: 
ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-497965 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetate--CoA ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 657 amino acids
Theoretical weight: 74.12 KDa
Source organism: Chloroflexota bacterium
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A535FEC2 (Residues: 2-647; Coverage: 100%)
Gene names: E6J36_13485, acs
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand K 1 x K
1 modified residue:
Ligand NEP 4 x NEP

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: R32
Unit cell:
a: 161.352Å b: 161.352Å c: 814.182Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.163 0.221
Expression system: Escherichia coli BL21

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Citations

1 citations in other articles

Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.
Qin et al. (2024)