› 1j0a

X-ray diffraction
2.5Å resolution

Crystal Structure Analysis of the ACC deaminase homologue

Released:
DOI: 10.2210/pdb1j0a/pdb
PDB entry 1j0a coloured by chain, front view.
PDB entry 1j0a coloured by chain, side view.
PDB entry 1j0a coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Structural and enzymatic properties of 1-aminocyclopropane-1-carboxylate deaminase homologue from Pyrococcus horikoshii.
Fujino A, Ose T, Yao M, Tokiwano T, Honma M, Watanabe N, Tanaka I
J Mol Biol 341 999-1013 (2004)
PMID: 15328614

Function and Biology Details

Reaction catalysed: 
(1a) 1-aminocyclopropane-1-carboxylate = 2-aminobut-2-enoate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-129614 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative 1-aminocyclopropane-1-carboxylate deaminase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 325 amino acids
Theoretical weight: 35.23 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O57809 (Residues: 1-325; Coverage: 100%)
Gene names: PH0054, PHBE027
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 3 x PLP
2 bound ligands:
Ligand SO4 3 x SO4
Ligand IPA 1 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: P3221
Unit cell:
a: 122.34Å b: 122.34Å c: 115.031Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.201 0.27
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Modulation of plant ethylene levels by the bacterial enzyme ACC deaminase.
Glick BR. (2005)
4 more

5 mentions without citation

Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus.
Beasley et al. (2011)
4 more