Structural basis for two metal-ion catalysis of DNA cleavage by Cas12i2
| Title | Structural basis for two metal-ion catalysis of DNA cleavage by Cas12i2 |
|---|---|
| Description | Cas12i2 is a Class 2 type V-I CRISPR-Cas endonuclease that cleaves target dsDNA by an unknown mechanism. We reveal the mechanism of DNA recognition and cleavage by Cas12i2, and activation of the RuvC catalytic pocket induced by a conformational change of the Helical-II domain. We captured the catalytic state of Cas12i2, with both metal ions and the ssDNA substrate bound in the RuvC catalytic pocket. Together, our studies provide significant insights into the DNA cleavage mechanism by RuvC-containing Cas proteins. |
| Organism | DNA-binding vector pODB80 |
| Data Type | Protein 3D Structure Data |
| Data Accessibility | Open-access |
| BioProject | PRJCA016730 |
| Release Date | 2023-05-05 |
| Submitter | Yunran Zhan (yunranzhan@ibp.ac.cn) |
| Organization | Institute of Biophysics Chinese Academy of Sciences |
| Submission Date | 2023-05-05 |
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| File ID | File Title | Number/Samples | File Type | File Size | File Suffix | Download Times | Download |
|---|---|---|---|---|---|---|---|
| OMIX003905-01 | Crystal structure of the Cas12i2 complex | 4 | Protein 3D Structure Data | 858.8 KB | zip | 0 |