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1.3.7.12: red chlorophyll catabolite reductase

This is an abbreviated version!
For detailed information about red chlorophyll catabolite reductase, go to the full flat file.

Word Map on EC 1.3.7.12

Reaction

primary fluorescent chlorophyll catabolite
+ 2 oxidized ferredoxin [iron-sulfur] cluster =
red chlorophyll catabolite
+ 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+

Synonyms

ACD2 protein, At-RCCR, AtRCCR, BoRCCR, BrRCCR, CaRCCR, EC 1.3.1.80, HvRCCR, PHAVU_008G280300g, RCC reductase, RCCR, RCCR-1, RCCR-2, red Chl catabolite reductase, red chlorophyll catabolite reductase, red-chlorophyll-catabolite reductase

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.7 With an iron-sulfur protein as acceptor
                1.3.7.12 red chlorophyll catabolite reductase

Crystallization

Crystallization on EC 1.3.7.12 - red chlorophyll catabolite reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.4 A resolution, determination of the crystal structure of, where chloroplast transit peptide is truncated and a Gly-Pro-Leu-Gly-Ser peptide is added to the N terminus, 2 peptide chains A and B are located in an asymmetric unit of the selenomethionine-RCCR crystal, these 2 chains form a homodimer, AtRCCR folds into an alpha/beta/alpha sandwich: 5 N-terminal alpha-helices, an anti-parallel beta-sheet consisting of 8 strands, and 4 C-terminal alpha-helices
purified recombinant RCC-bound wild-type enzyme AtRCCRDELTA49, RCC-bound and substrate-free enzyme mutant F218V AtRCCRDELTA49, sitting-drop vapor diffusion method, mixing of 10 mg/ml substrate-free and substrate-bound proteins in 20 mM Tris-HCl, pH 7.4, and 200 mM NaCl, with an equal volume of reservoir solution containing 30% or 35%, respectively, w/v PEG 2000 monomethyl ether, 0.1 M ammonium acetate, 3% v/v dioxane, and 0.1 M 4-morpholineethanesulfonic acid-NaOH, pH 6.5, equilibration gainst reservoir solution, 20°C, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution
purified recombinant red chlorophyll catabolite-bound RCCRDELTA49, and red chlorophyll catabolite-bound or substrate-free F218V RCCRDELTA49, sitting drop vapor diffusion method, 20°C, protein solution is mixed with an equal volume of reservoir solution and equilibrated against reservoir solution containing 30% w/v PEG 2000 monomethyl ether, 0.1 M ammonium acetate, 3% v/v dioxane, and 0.1 M 4-morpholineethanesulfonic acid-NaOH, pH 6.5, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution
purified substrate-free enzyme, with the chloroplast transit peptide truncated and a Gly-Pro-Leu-Gly-Ser peptide added to the N-terminus, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution, structure modelling