BpuJI
| BpuJI N terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | BpuJI_N | ||||||||
| Pfam | PF11564 | ||||||||
| InterPro | IPR021108 | ||||||||
| |||||||||
In molecular biology, BpuJI is a type II restriction endonuclease which recognises the asymmetric sequence 5'-CCCGT and cuts at multiple sites in the surrounding area of the target sequence. The BpuJI protein consists of two distinct modules; an N-terminal DNA recognition domain, and a C-terminal dimerisation and catalysis domain. The N-terminal domain is composed of two winged-helix subdomains and a disrupted linker subdomain. Target sequence recognition occurs through major groove contacts of amino acids in the winged-helix subdomains.[1]
References[]
- ^ Sukackaite R, Grazulis S, Bochtler M, Siksnys V (May 2008). "The recognition domain of the BpuJI restriction endonuclease in complex with cognate DNA at 1.3-A resolution". J. Mol. Biol. 378 (5): 1084â–93. doi:10.1016/j.jmb.2008.03.041. PMID 18433771.
Categories:
- Protein families
- Molecular biology
- Bacterial enzymes
- Restriction enzymes
- EC 3.1