R.EcoRII

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File:Eco RII 1NA6.png
Eco RII dimer based on PDB ID 1NA6

EcoRII (pronounced 'eco R two') is an Restriction endonuclease enzyme (REase) of the restriction modification system (RM) naturally found in Escherichia coli, a Gram-negative bacteria. Its molecular mass is 45.2 kDa, being composed of 402 amino acids.[1]

Mode of action

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EcoRII is a bacterial Type IIE[2] REase that interacts with two[3] or three[4] 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.[5]

Cut diagram

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Recognition site Cut results
5' NNCCWGGNN
3' NNGGWCCNN 
5' NN  CCWGGNN
3' NNGGWCC  NN

Structure

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Restriction endonuclease EcoRII, N-terminal
File:PDB 1na6 EBI.jpg
crystal structure of restriction endonuclease ecorii mutant r88a
Identifiers
SymbolEcoRII-N
PfamPF09217
Pfam clanCL0405
InterProIPR015300
SCOP21na6 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
EcoRII C terminal
File:PDB 1na6 EBI.jpg
crystal structure of restriction endonuclease ecorii mutant r88a
Identifiers
SymbolEcoRII-C
PfamPF09019
Pfam clanCL0236
InterProIPR015109
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The apo crystal structure of EcoRII mutant R88A (PDB: 1NA6​)[6] 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

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The N-terminal effector-binding domain has an archetypal DNA-binding pseudobarrel fold (SCOP 101936) with a prominent cleft. Structural superposition showed it is evolutionarily related to:

Catalytic domain

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The C-terminal catalytic domain has a typical[10] restriction endonuclease-like fold (SCOP 52979) and belongs to the large (more than 30 members) restriction endonuclease superfamily (SCOP 52980).

Autoinhibition/activation mechanism

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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.[6]

See also

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  • EcoRII in Restriction Enzyme Database REBASE

References

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