Structure of restriction endonuclease BamHI and its relationship to EcoRI

@article{Newman1994StructureOR,
  title={Structure of restriction endonuclease BamHI and its relationship to EcoRI},
  author={M. Newman and Teresa E. Strzelecka and Lydia F. Dorner and Ira Schildkraut and Aneel K. Aggarwal},
  journal={Nature},
  year={1994},
  volume={368},
  pages={660-664}
}
TYPE II restriction endonucleases are characterized by the remarkable specificity with which they cleave specific DNA sequences. Surprisingly, their protein sequences are in most cases unrelated, and no recurring structural motif has yet been identified1,2. We have determined the structure of restriction endonuclease BamHI at 1.95 Å resolution. BamHI shows striking resemblance to the structure of endonuclease EcoRI (refs 3, 4), despite the lack of sequence similarity between them. We also… Expand
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  • Biology, Medicine
  • Current opinion in structural biology
  • 1995
TLDR
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Structure of restriction endonuclease bamhi phased at 1.95 A resolution by MAD analysis.
TLDR
The structure of BamHI provides the first clear evidence that there may be substantial structural homology amongst restriction enzymes, even though it is undetectable at the sequence level. Expand
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The role of metals in catalysis by the restriction endonuclease Bam HI
TLDR
Structures of the endonuclease BamHI–DNA complex, determined in the presence of Mn2+ and Ca2+, that describe the enzyme at different stages of catalysis support a two-metal mechanism of DNA cleavage for BamHI which is distinct from that of EcoRV. Expand
Evolutionary relationship of Alw26I, Eco31I and Esp3I, restriction endonucleases that recognise overlapping sequences
TLDR
The cloning and sequence analysis of genes for three Type IIS restriction-modification (RM) systems show the degree of sequence identity between Alw26I, Eco31I and Esp3I ENases is higher than that observed hitherto among ENases that recognise partially overlapping nucleotide sequences. Expand
Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold.
TLDR
The structure together with the earlier characterized EcoRII enzyme activity enhancement in the absence of its N-terminal domain reveal an autoinhibition/activation mechanism of enzyme activity mediated by a novel effector-binding fold, the first case of autoinhibited mechanism described for many transcription factors and signal transducing proteins, of a restriction endonuclease. Expand
Recognition and cleavage of DNA by type-II restriction endonucleases.
TLDR
Structural similarities identified between EcoRI, EcoRV, BamHI, PvuII and Cfr10I suggest that many type II restriction endonucleases are not only functionally but also evolutionarily related. Expand
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