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| Item Type: | Article |
|---|---|
| Title: | High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI |
| Creators Name: | Werner, E. and Wende, W. and Pingoud, A. and Heinemann, U. |
| Abstract: | The homing endonuclease PI-SceI from Saccharo myces cerevisiae consists of two domains. The protein splicing domain I catalyzes the excision of the mature endonuclease (intein) from a precursor protein and the religation of the flanking amino acid sequences (exteins) to a functional protein. Furthermore, domain I is involved in binding and recognition of the specific DNA substrate. Domain II of PI-SceI, the endonuclease domain, which is structurally homologous to other homing endonucleases from the LAGLIDADG family, harbors the endonucleolytic center of PI-SceI, which in vivo initiates the homing process by introducing a double-strand cut in the approximately 35 bp recognition sequence. At 1.35 A resolution, the crystal structure of PI-SceI domain I provides a detailed view of the part of the protein that is responsible for tight and specific DNA binding. A geometry-based docking of the 75 degrees bent recognition sequence to the full-length protein implies a conformational change or hinge movement of a subdomain of domain I, the tongs part, that is predicted to reach into the major groove near base pairs +16 to +18. |
| Keywords: | Binding Sites, X-Ray Crystallography, Endodeoxyribonucleases, Fungal Proteins, Molecular Models, Protein Conformation, Protein Splicing, Tertiary Protein Structure, Proton-Translocating AT, Pases, Saccharomyces Cerevisiae Proteins |
| Source: | Nucleic Acids Research |
| ISSN: | 0305-1048 |
| Publisher: | Oxford University Press |
| Volume: | 30 |
| Number: | 18 |
| Page Range: | 3962-3971 |
| Date: | 15 September 2002 |
| Official Publication: | https://doi.org/10.1093/nar/gkf523 |
| PubMed: | View item in PubMed |
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