R.EcoRII

EcoRII is a bacterial Type IIE REase that interacts with two or three copies of the pseudopalindromic DNA recognition sequence 5'-CCWGG-3' (W = A or T), one being the actual target of cleavage, the other(s) serving as the allosteric activator(s). EcoRII cuts the target DNA sequence CCWGG, generating sticky ends. ==Cut diagram==

The apo crystal structure of EcoRII mutant R88A () has been solved at 2.1 Å resolution. The EcoRII monomer has two domains, N-terminal and C-terminal, linked through a hinge loop. Effector-binding domain The N-terminal effector-binding domain has an archetypal DNA-binding pseudobarrel fold () with a prominent cleft. Structural superposition showed it is evolutionarily related to: • B3 DNA binding domain () from the transcription factors in higher plants () • C-terminal domain of restriction endonuclease BfiI () Catalytic domain The C-terminal catalytic domain has a typical restriction endonuclease-like fold () and belongs to the large (more than 30 members) restriction endonuclease superfamily (). ==Autoinhibition/activation mechanism==

Structure-based sequence alignment and site-directed mutagenesis identified the putative PD..D/EXK active sites of the EcoRII catalytic domain dimer that in apo structure are spatially blocked by the N-terminal domains. ==See also==