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BRENDA support

Literature summary for 4.1.99.3 extracted from

  • Hitomi, K.; Arvai, A.S.; Yamamoto, J.; Hitomi, C.; Teranishi, M.; Hirouchi, T.; Yamamoto, K.; Iwai, S.; Tainer, J.A.; Hidema, J.; Getzoff, E.D.
    Eukaryotic class II cyclobutane pyrimidine dimer photolyase structure reveals basis for improved ultraviolet tolerance in plants (2012), J. Biol. Chem., 287, 12060-12069.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of GST-tagged enzyme Oryza sativa Japonica Group

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant detagged enzyme, hanging drop vapor diffusion method, protein in 50 mM Tris-HCl (pH 8.0), 50 mM NaCl, 1 mM DTT, and 5% glycerol is mixed with 100 mM sodium cacodylate, pH 6.5, 200 mM ammonium sulfate, and 30% w/v PEG 8000 for crystal form I, and with 32% w/v PEG 4000, 5% urea, 100 mM imidazole/malate, pH 7.4 for crystal form II, 4°C, X-ray diffraction structure determination and analysis at 1.7 A resolution Oryza sativa Japonica Group

Organism

Organism UniProt Comment Textmining
Oryza sativa Japonica Group Q6F6A2 cultivar Sasanishiki
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Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged enzyme, the GST is cleaved by treatment with thrombin at 25°C for 2 h and removed by using a heparin column Oryza sativa Japonica Group

Reaction

Reaction Comment Organism Reaction ID
cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA) substrate/cofactor binding and reaction mechanism, catalytic active site Met397, overview Oryza sativa Japonica Group

Synonyms

Synonyms Comment Organism
CPD2PHR
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Oryza sativa Japonica Group
eukaryotic Class II CPD PHR
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Oryza sativa Japonica Group
eukaryotic class II cyclobutane pyrimidine dimer photolyase
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Oryza sativa Japonica Group
PHR
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Oryza sativa Japonica Group

Cofactor

Cofactor Comment Organism Structure
FAD the C-terminal domain frames a concave pocket that holds the FAD cofactor in the U-shaped conformation. The U-shaped FAD is positioned with the isoalloxazine ring buried and the adenine ring solvent-exposed beneath the substrate binding pocket. A salt bridge (Arg396 to Asp427) across the isoalloxazine ring orients the guanidinium to stabilize a semiquinone radical at the C4a position. Cofactor binding and interactions with the enzyme, overview Oryza sativa Japonica Group

General Information

General Information Comment Organism
evolution the PHR/CRY family consists of two major classes, class I and class II, the enzyme from rice belongs to class II Oryza sativa Japonica Group
additional information structure-activity relationships in class II PHRs, overview. Structural comparisons with prokaryotic class I CPD PHRs identify differences in the binding site for UV-damaged DNA substrate Oryza sativa Japonica Group