Literature summary for 3.1.21.3 extracted from

Lapkouski, M.; Panjikar, S.; Janscak, P.; Smatanova, I.K.; Carey, J.; Ettrich, R.; Csefalvay, E.
Structure of the motor subunit of type I restriction-modification complex EcoR124I (2009), Nat. Struct. Mol. Biol., 16, 94-95.

Cloned(Commentary)

Cloned (Comment)	Organism
EcoR124I HsdR with selenomethionine labeling expressed in Escherichia coli	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
motor subunit HsdR of pR124 plasmid-borne type I restriction-modification enzyme EcoR124I, solved in complex with Mg2+-ATP at 2.6 A resolution. HsdR presents four globular domains in a square-planar arrangement, generating prominent grooves between adjacent domain pairs. Lys220 on alpha8 is 3.1 A from N3 on the exposed edge of ATP bound at the helicase domains, potentially coupling endonuclease and helicase function. A uniformly positive surface groove with a clear match to the size and shape of duplex DNA proceeds from a canonical helicase cleft in a continuous path down the front of the motor subunit between the helical and endonuclease domains, where the cleavage site is recessed slightly from the surface	Escherichia coli

Crystallization (Comment)

Organism

motor subunit HsdR of pR124 plasmid-borne type I restriction-modification enzyme EcoR124I, solved in complex with Mg2+-ATP at 2.6 A resolution. HsdR presents four globular domains in a square-planar arrangement, generating prominent grooves between adjacent domain pairs. Lys220 on alpha8 is 3.1 A from N3 on the exposed edge of ATP bound at the helicase domains, potentially coupling endonuclease and helicase function. A uniformly positive surface groove with a clear match to the size and shape of duplex DNA proceeds from a canonical helicase cleft in a continuous path down the front of the motor subunit between the helical and endonuclease domains, where the cleavage site is recessed slightly from the surface

Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q304R3	-	-

Subunits

Subunits	Comment	Organism
pentamer	crystallography	Escherichia coli

Synonyms

Synonyms	Comment	Organism
EcoR124I	-	Escherichia coli
type I restriction-modification enzyme	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)