The metal-independent type IIs restriction enzyme BfiI is a dimer that binds two DNA sites but has only one catalytic centre.
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Structure of the metal-independent restriction enzyme BfiI reveals fusion of a specific DNA-binding domain with a nonspecific nucleaseCatalytic domain of restriction endonuclease BmrI as a cleavage module for engineering endonucleases with novel substrate specificitiesRestriction endonuclease BpuJI specific for the 5'-CCCGT sequence is related to the archaeal Holliday junction resolvase familyA homology model of restriction endonuclease SfiI in complex with DNAStructure of HinP1I endonuclease reveals a striking similarity to the monomeric restriction enzyme MspI.Protein assembly and DNA looping by the FokI restriction endonuclease.Characterization and crystal structure of the type IIG restriction endonuclease RM.BpuSIStructural insight into the specificity of the B3 DNA-binding domains provided by the co-crystal structure of the C-terminal fragment of BfiI restriction enzymeStructure of 5-hydroxymethylcytosine-specific restriction enzyme, AbaSI, in complex with DNACharacterization of multi-functional properties and conformational analysis of MutS2 from Thermotoga maritima MSB8A genetic dissection of the LlaJI restriction cassette reveals insights on a novel bacteriophage resistance systemTemplate-directed addition of nucleosides to DNA by the BfiI restriction enzymeType II restriction endonucleases--a historical perspective and moreDNA synapsis through transient tetramerization triggers cleavage by Ecl18kI restriction enzyme.Natural and engineered nicking endonucleases--from cleavage mechanism to engineering of strand-specificityA type IV modification-dependent restriction enzyme SauUSI from Staphylococcus aureus subsp. aureus USA300How the BfiI restriction enzyme uses one active site to cut two DNA strands.Characterization of LlaKI, a New Metal Ion-Independent Restriction Endonuclease from Lactococcus lactis KLDS4.Phospholipase D: enzymology, functionality, and chemical modulationSite-specific DNA transesterification catalyzed by a restriction enzyme.Nucleases: diversity of structure, function and mechanism.Target site cleavage by the monomeric restriction enzyme BcnI requires translocation to a random DNA sequence and a switch in enzyme orientation.Crystal structure of the R-protein of the multisubunit ATP-dependent restriction endonuclease NgoAVII.DNA supercoiling enables the type IIS restriction enzyme BspMI to recognise the relative orientation of two DNA sequencesA novel mechanism for the scission of double-stranded DNA: BfiI cuts both 3'-5' and 5'-3' strands by rotating a single active siteOne recognition sequence, seven restriction enzymes, five reaction mechanisms.Restriction endonucleases that bridge and excise two recognition sites from DNA.Tetrameric restriction enzymes: expansion to the GIY-YIG nuclease family.Differences between Ca2+ and Mg2+ in DNA binding and release by the SfiI restriction endonuclease: implications for DNA looping.Identification of a single HNH active site in type IIS restriction endonuclease Eco31I.Degenerate sequence recognition by the monomeric restriction enzyme: single mutation converts BcnI into a strand-specific nicking endonuclease.DNA cleavage by CgII and NgoAVII requires interaction between N- and R-proteins and extensive nucleotide hydrolysis.Identification and mutational analysis of Mg2+ binding site in EcoP15I DNA methyltransferase: involvement in target base eversion.UbaLAI is a monomeric Type IIE restriction enzyme.Biochemical and mutational analysis of EcoRII functional domains reveals evolutionary links between restriction enzymes.
P2860
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P2860
The metal-independent type IIs restriction enzyme BfiI is a dimer that binds two DNA sites but has only one catalytic centre.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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name
The metal-independent type IIs ...... has only one catalytic centre.
@en
type
label
The metal-independent type IIs ...... has only one catalytic centre.
@en
prefLabel
The metal-independent type IIs ...... has only one catalytic centre.
@en
P2093
P1476
The metal-independent type IIs ...... has only one catalytic centre.
@en
P2093
Arunas Lagunavicius
Giedrius Sasnauskas
Stephen E Halford
Virginijus Siksnys
P304
P356
10.1016/S0022-2836(03)00020-2
P407
P577
2003-02-01T00:00:00Z