2C1L

Structure of the BfiI restriction endonuclease

Summary for 2C1L

• Entry DOI: 10.2210/pdb2c1l/pdb
• Descriptor: RESTRICTION ENDONUCLEASE, GLYCEROL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (9 entities in total)
• Functional Keywords: bfii, restriction endonuclease, domain fusion, hydrolase
• Biological source: BACILLUS FIRMUS
• Total number of polymer chains: 2
• Total formula weight: 81836.59

Authors

Grazulis, S.,Manakova, E.,Roessle, M.,Bochtler, M.,Tamulaitiene, G.,Huber, R.,Siksnys, V. (deposition date: 2005-09-15, release date: 2005-10-07, Last modification date: 2024-05-08)

Primary citation

Grazulis, S.,Manakova, E.,Roessle, M.,Bochtler, M.,Tamulaitiene, G.,Huber, R.,Siksnys, V.
Structure of the Metal-Independent Restriction Enzyme Bfii Reveals Fusion of a Specific DNA-Binding Domain with a Nonspecific Nuclease.
Proc.Natl.Acad.Sci.USA, 102:15797-, 2005

PubMed Abstract: Among all restriction endonucleases known to date, BfiI is unique in cleaving DNA in the absence of metal ions. BfiI represents a different evolutionary lineage of restriction enzymes, as shown by its crystal structure at 1.9-A resolution. The protein consists of two structural domains. The N-terminal catalytic domain is similar to Nuc, an EDTA-resistant nuclease from the phospholipase D superfamily. The C-terminal DNA-binding domain of BfiI exhibits a beta-barrel-like structure very similar to the effector DNA-binding domain of the Mg(2+)-dependent restriction enzyme EcoRII and to the B3-like DNA-binding domain of plant transcription factors. BfiI presumably evolved through domain fusion of a DNA-recognition element to a nonspecific nuclease akin to Nuc and elaborated a mechanism to limit DNA cleavage to a single double-strand break near the specific recognition sequence. The crystal structure suggests that the interdomain linker may act as an autoinhibitor controlling BfiI catalytic activity in the absence of a specific DNA sequence. A psi-blast search identified a BfiI homologue in a Mesorhizobium sp. BNC1 bacteria strain, a plant symbiont isolated from an EDTA-rich environment.

PubMed: 16247004
DOI: 10.1073/PNAS.0507949102

Experimental method

X-RAY DIFFRACTION (1.9 Å)