Literature summary for 3.1.21.2 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.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants

Protein Variants	Comment	Organism
E118A	site-directed mutagenesis	Tequatrovirus T4

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Tequatrovirus T4	-	gene denA	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
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
tetramer	4 * 16000	Tequatrovirus T4

Synonyms

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

General Information

General Information	Comment	Organism
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