› 1ynu

X-ray diffraction
2.25Å resolution

Crystal structure of apple ACC synthase in complex with L-vinylglycine

Released:
DOI: 10.2210/pdb1ynu/pdb
PDB entry 1ynu coloured by chain, front view.
PDB entry 1ynu coloured by chain, side view.
PDB entry 1ynu coloured by chain, top view.
Source organism: Malus domestica
Primary publication:
Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine.
Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grütter MG
FEBS Lett 579 2458-62 (2005)
PMID: 15848188

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + S-methyl-5'-thioadenosine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153492 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-aminocyclopropane-1-carboxylate synthase Chain: A
Molecule details ›
Chain: A
Length: 473 amino acids
Theoretical weight: 53.31 KDa
Source organism: Malus domestica
Expression system: Escherichia coli
UniProt:
  • Canonical: P37821 (Residues: 1-473; Coverage: 100%)
Gene name: ACS-1
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand NI 2 x NI
Ligand K 1 x K
Ligand PY4 1 x PY4
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 103.3Å b: 59.36Å c: 79.05Å
α: 90° β: 124.2° γ: 90°
R-values:
R R work R free
0.234 0.234 0.289
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural insights into radical generation by the radical SAM superfamily.
Vey et al. (2011)
9 other articles

2 mentions without citation

α-Vinylic Amino Acids: Occurrence, Asymmetric Synthesis and Biochemical Mechanisms.
Berkowitz et al. (2006)
1 more