Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence

@article{Moure2002CrystalSO,
  title={Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence},
  author={Carmen M. Moure and Frederick S. Gimble and Florante A. Quiocho},
  journal={Nature Structural Biology},
  year={2002},
  volume={9},
  pages={764-770}
}
The first X-ray structures of an intein–DNA complex, that of the two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA substrate, have been determined in the presence and absence of Ca2+. The DNA shows an asymmetric bending pattern, with a major 50° bend in the endonuclease domain and a minor 22° bend in the splicing domain region. Distortions of the DNA bound to the endonuclease domain cause the insertion of the two cleavage sites in the catalytic center. DNA binding induces… 
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TLDR
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TLDR
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TLDR
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Homology modeling and mutational analysis of Ho endonuclease of yeast.
TLDR
A homology model for Ho and mutational analysis indicated that residues in Ho that are conserved relative to catalytic, active-site residues in PI-SceI and other related homing endonucleases are essential for Ho activity.
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TLDR
It is suggested that the cleavage of each strand is catalyzed by each of the two non-equivalent active sites of PI-PfuI.
The structure of I-Crel, a Group I intron-encoded homing endonuclease
TLDR
The structure of I-Crel provides the first view of a protein encoded by a gene within an intron and the conserved LAGLIDADG motif, found in many mobile intron endonucleases, maturases and inteins, forms a novel helical interface and contributes essential residues to the active site.
Crystal Structure of PI-SceI, a Homing Endonuclease with Protein Splicing Activity
TLDR
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A Mutational Analysis of DNA Binding and Cleavage by the Homing Endonuclease PI-SceI
TLDR
A model is presented for DNA binding and cleavage by PI-SceI, the best studied intein-like homing endonuclease of the LAGLIDADG family, to find out which amino acid residues are involved in substrate binding and processing.
Mapping of a DNA binding region of the PI-sceI homing endonuclease by affinity cleavage and alanine-scanning mutagenesis.
The PI-SceI protein is a member of the LAGLIDADG family of homing endonucleases that is generated by a protein splicing reaction. PI-SceI has a bipartite domain structure, and the protein splicing
Photocross-linking of the Homing Endonuclease PI-SceI to Its Recognition Sequence*
TLDR
To define the DNA binding site of PI-SceI, photocross-linking was used to identify amino acid residues in contact with DNA, and the finding that at least one His residue is in close contact to the DNA was supported.
The protein splicing domain of the homing endonuclease PI-sceI is responsible for specific DNA binding.
TLDR
Results indicate that protein splicing domain I is also involved in recognition of the DNA substrate, and specifically to the PI- Sce I recognition sequence.
Substrate recognition and induced DNA distortion by the PI-SceI endonuclease, an enzyme generated by protein splicing.
TLDR
A model is proposed in which sequence-specific contacts made by PI-SceI contribute to its localization to the cleavage site and to its stabilization of a DNA conformation that is required for catalysis, which may have allowed the evolution of other endonucleases with altered, but similar, specificities.
The homing endonuclease I-CreI uses three metals, one of which is shared between the two active sites
Homing endonucleases, like restriction enzymes, cleave double-stranded DNA at specific target sites. The cleavage mechanism(s) utilized by LAGLIDADG endonucleases have been difficult to elucidate;
Probing the Structure of the PI-SceI-DNA Complex by Affinity Cleavage and Affinity Photocross-linking*
TLDR
A new PI-SceI structure that is ordered in regions of the protein that bind DNA is used, and the results suggest that an extended β-hairpin loop in the endonuclease domain that contains residues 376 and 378 contacts the major groove near the PI- SceI cleavage site.
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