› 1j0e

X-ray diffraction
2.45Å resolution

ACC deaminase mutant reacton intermediate

Released:
DOI: 10.2210/pdb1j0e/pdb
PDB entry 1j0e coloured by chain, front view.
PDB entry 1j0e coloured by chain, side view.
PDB entry 1j0e coloured by chain, top view.
Source organism: Cyberlindnera saturnus
Primary publication:
Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction.
Ose T, Fujino A, Yao M, Watanabe N, Honma M, Tanaka I
J Biol Chem 278 41069-76 (2003)
PMID: 12882962

Function and Biology Details

Reaction catalysed: 
(1a) 1-aminocyclopropane-1-carboxylate = 2-aminobut-2-enoate
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-181704 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1-aminocyclopropane-1-carboxylate deaminase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 341 amino acids
Theoretical weight: 37.07 KDa
Source organism: Cyberlindnera saturnus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7M523 (Residues: 1-341; Coverage: 100%)
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:
Ligand 1AC 4 x 1AC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 65.4Å b: 269.586Å c: 186.913Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.263
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Bacteria with ACC deaminase can promote plant growth and help to feed the world.
Glick BR. (2014)
7 more

1 mention without citation

Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase.
Bharath et al. (2012)