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Literature summary extracted from

  • Morikawa, K.; Shirakawa, M.
    Three-dimensional structural views of damaged-DNA recognition: T4 endonuclease V, E. coli Vsr protein, and human nucleotide excision repair factor XPA (2000), Mutat. Res., 460, 257-275.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.25.1 overexpression in Escherichia coli Tequatrovirus T4

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.25.1 purified recombinant enzyme and mutants in complex with DNA containing a thymidine-dimer, X-ray diffraction structure determination and analysis at 1.45-1.6 A and 2.75 A resolution, the latter by molecular replacement method Tequatrovirus T4

Protein Variants

EC Number Protein Variants Comment Organism
3.1.25.1 E23D active site mutant, retains full substrate binding ability but shows complex structure differences, crystal structure determination with a bound DNA duplex in comparison to the wild-type enzyme Tequatrovirus T4
3.1.25.1 E23Q active site mutant, retains full substrate binding ability but shows complex structure differences, crystal structure determination with a bound DNA duplex in comparison to the wild-type enzyme Tequatrovirus T4
3.1.25.1 R3Q active site mutant, retains full substrate binding ability but shows complex structure differences, crystal structure determination with a bound DNA duplex in comparison to the wild-type enzyme Tequatrovirus T4

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.25.1 DNA + H2O Tequatrovirus T4 first reaction step of the repair pathway to excise pyrimidine-dimers ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.25.1 Tequatrovirus T4
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.25.1 recombinant from Escherichia coli Tequatrovirus T4

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.25.1 endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate damaged DNA substrate recognition mechanism, 2 distinct catalytic activities: cleavage of the glycosyl bond at the 5'side of pyrimidine dimer and subsequent scission of the phosphodiester bond at the 3' position of an abasic site through beta-elimination, the enzyme also scans nontarget sequences to search for lesions in DNA duplexes, glycosylase active site involves the catalytic residues Arg3, Glu23, Arg22, and Arg26 and the amino terminus which forms an imino-covalent intermediate with C1' of the 5' side of the thymidine-dimer Tequatrovirus T4
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.25.1 DNA + H2O first reaction step of the repair pathway to excise pyrimidine-dimers Tequatrovirus T4 ?
-
 ?
3.1.25.1 DNA + H2O excision of thymine dimers produced within duplex DNA by UV radiation Tequatrovirus T4 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.25.1 More the 2 enzyme activities are located in one compact domain consisting of 3 alpha helices and a connecting loop Tequatrovirus T4

Synonyms

EC Number Synonyms Comment Organism
3.1.25.1 bacteriophage T4 endodeoxyribonuclease V
-
 Tequatrovirus T4
3.1.25.1 endodeoxyribonuclease (pyrimidine dimer)
-
 Tequatrovirus T4
3.1.25.1 T4 Endo V
-
 Tequatrovirus T4
3.1.25.1 T4 endonuclease V
-
 Tequatrovirus T4