2c1l
From Proteopedia
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'''STRUCTURE OF THE BFII RESTRICTION ENDONUCLEASE''' | '''STRUCTURE OF THE BFII RESTRICTION ENDONUCLEASE''' | ||
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[[Category: Siksnys, V.]] | [[Category: Siksnys, V.]] | ||
[[Category: Tamulaitiene, G.]] | [[Category: Tamulaitiene, G.]] | ||
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| - | [[Category: | + | [[Category: Hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:06:21 2008'' | |
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Revision as of 18:06, 3 May 2008
STRUCTURE OF THE BFII RESTRICTION ENDONUCLEASE
Overview
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.
About this Structure
2C1L is a Single protein structure of sequence from Bacillus firmus. Full crystallographic information is available from OCA.
Reference
Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nuclease., Grazulis S, Manakova E, Roessle M, Bochtler M, Tamulaitiene G, Huber R, Siksnys V, Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15797-802. Epub 2005 Oct 24. PMID:16247004 Page seeded by OCA on Sat May 3 21:06:21 2008
