› 3agc

X-ray diffraction
2Å resolution

F218V mutant of the substrate-bound red chlorophyll catabolite reductase from Arabidopsis thaliana

Released:
DOI: 10.2210/pdb3agc/pdb
PDB entry 3agc coloured by chain, front view.
PDB entry 3agc coloured by chain, side view.
PDB entry 3agc coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Crystal structures of the substrate-bound forms of red chlorophyll catabolite reductase: implications for site-specific and stereospecific reaction.
Sugishima M, Okamoto Y, Noguchi M, Kohchi T, Tamiaki H, Fukuyama K
J Mol Biol 402 879-91 (2010)
PMID: 20727901

Function and Biology Details

Reaction catalysed: 
Primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185283 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Red chlorophyll catabolite reductase, chloroplastic Chains: A, B
Molecule details ›
Chains: A, B
Length: 276 amino acids
Theoretical weight: 31.35 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8LDU4 (Residues: 49-319; Coverage: 85%)
Gene names: ACD2, At4g37000, C7A10_360, RCCR
Sequence domains: Red chlorophyll catabolite reductase (RCC reductase)
Structure domains: oxygen-dependent coproporphyrinogen oxidase

Ligands and Environments

2 bound ligands:
Ligand RCC 1 x RCC
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 45.089Å b: 84.321Å c: 131.518Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.209 0.27
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Update on the biochemistry of chlorophyll breakdown.
Hörtensteiner S. (2013)
3 more

2 mentions without citation

Investigations Concerning the Syntheses of TADDOL-Derived Secondary Amines and Their Use To Access Novel Chiral Organocatalysts.
Gratzer et al. (2012)
1 more