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Literature summary extracted from

  • Andersson, C.E.; Lagerbaeck, P.; Carlson, K.
    Structure of bacteriophage T4 endonuclease II mutant E118A, a tetrameric GIY-YIG enzyme (2010), J. Mol. Biol., 397, 1003-1016.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.21.8 expression in Escherichia coli Tequatrovirus T4

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.21.2 mutant E118A of EndoII is crystallized in space group P21 with four monomers in the asymmetric unit, with a bound phosphate ion in one of the four active sites of EndoII likely mimicing the scissile phosphate in a true substrate complex. Crystallization of the selenomethionine-substituted E118A mutant, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution, molecular replacement Tequatrovirus T4
3.1.21.8 mutant E118A,crystallized in space group P21 with four monomers in the asymmetric unit. EndoII forms a striking X-shaped tetrameric structure composed as a dimer of dimers, with a protruding hairpin domain providing most of the dimerization and tetramerization interfaces. A bound phosphate ion in one of the four active sites of EndoII likely mimics the scissile phosphate in a true substrate complex. A protruding loop containing a nuclease-associated modular domain 3 element is likely to be involved in substrate binding, as well as residues forming a separate nucleic acid binding surface adjacent to the active site. The substrate would bind to a primary EndoII dimer diagonally over the active sites, requiring significant distortion of the enzyme or the substrate DNA, or both, for simultaneous nicking of both DNA strands. EndoII may bind its substrate inefficiently across the two sites in the dimer, offering a plausible explanation for the catalytic preponderance of single-strand nicks Tequatrovirus T4

Protein Variants

EC Number Protein Variants Comment Organism
3.1.21.2 E118A site-directed mutagenesis Tequatrovirus T4
3.1.21.8 E118A crystallization data Tequatrovirus T4

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.21.2 16000
-
 4 * 16000 Tequatrovirus T4

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.21.2 additional information Tequatrovirus T4 EndoII primarily catalyzes single-stranded nicking of DNA, 5 to 10fold less frequently double-stranded breaks are produced ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.2 Tequatrovirus T4
-
 gene denA
-
3.1.21.8 Tequatrovirus T4 P07059
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.2 additional information EndoII primarily catalyzes single-stranded nicking of DNA, 5 to 10fold less frequently double-stranded breaks are produced Tequatrovirus T4 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.21.2 More EndoII forms a striking X-shaped tetrameric structure composed as a dimer of dimers, with a protruding hairpin domain not present in UvrC or I-TevI providing most of the dimerization and tetramerization interfaces. Monomer structure and topology, quarternary structure, overview Tequatrovirus T4
3.1.21.2 tetramer 4 * 16000 Tequatrovirus T4

Synonyms

EC Number Synonyms Comment Organism
3.1.21.2 coliphage T4 endonuclease II
-
 Tequatrovirus T4
3.1.21.2 EndoII
-
 Tequatrovirus T4
3.1.21.2 More the enzyme belongs to the GIY-YIG family of endonucleases Tequatrovirus T4
3.1.21.8 denA
-
 Tequatrovirus T4
3.1.21.8 endonuclease II
-
 Tequatrovirus T4
3.1.21.8 GIY-YIG enzyme
-
 Tequatrovirus T4

General Information

EC Number General Information Comment Organism
3.1.21.2 additional information a protruding loop containing a nuclease-associated modular domain 3 element is likely to be involved in substrate binding, as well as residues forming a separate nucleic acid binding surface adjacent to the active site. EndoII may bind its substrate inefficiently across the two sites in the dimer, offering a plausible explanation for the catalytic preponderance of single-strand nicks Tequatrovirus T4