2c1l: Difference between revisions
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==Overview== | ==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 ... | 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== | ==About this Structure== | ||
2C1L is a | 2C1L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_firmus Bacillus firmus] with TAR, BCT, TRS, TLA, SRT, MES and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C1L OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: restriction endonuclease]] | [[Category: restriction endonuclease]] | ||
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Revision as of 16:12, 5 November 2007
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STRUCTURE OF THE BFII RESTRICTION ENDONUCLEASE
OverviewOverview
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 StructureAbout this Structure
2C1L is a Single protein structure of sequence from Bacillus firmus with TAR, BCT, TRS, TLA, SRT, MES and GOL as ligands. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
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
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