› 1iyn

X-ray diffraction
1.6Å resolution

Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights for its instability

Released:
DOI: 10.2210/pdb1iyn/pdb
PDB entry 1iyn coloured by chain, front view.
PDB entry 1iyn coloured by chain, side view.
PDB entry 1iyn coloured by chain, top view.
Source organism: Nicotiana tabacum
Primary publication:
Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights into its instability.
Wada K, Tada T, Nakamura Y, Ishikawa T, Yabuta Y, Yoshimura K, Shigeoka S, Nishimura K
J Biochem 134 239-44 (2003)
PMID: 12966073

Function and Biology Details

Reactions catalysed: 
(1a) 2 L-ascorbate + H(2)O(2) + 2 H(+) = 2 monodehydroascorbate + 2 H(2)O
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185296 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Plant heme peroxidase family profile domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 32.28 KDa
Source organism: Nicotiana tabacum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8LNY5 (Residues: 1-295; Coverage: 100%)
Gene name: sapx
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P212121
Unit cell:
a: 37.188Å b: 76.79Å c: 98.776Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.222
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Lactoperoxidase: structural insights into the function,ligand binding and inhibition.
Sharma et al. (2013)
2 more

9 mentions without citation

Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.
Zámocký et al. (2014)
8 more