Literature summary for 3.1.21.8 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.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Tequatrovirus T4

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
E118A	crystallization data	Tequatrovirus T4

Organism

Organism	UniProt	Comment	Textmining
Tequatrovirus T4	P07059	-	-

Synonyms

Synonyms	Comment	Organism
denA	-	Tequatrovirus T4
endonuclease II	-	Tequatrovirus T4
GIY-YIG enzyme	-	Tequatrovirus T4

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Release 2023.1 (January 2023)