4P6I
Crystal structure of the Cas1-Cas2 complex from Escherichia coli
Summary for 4P6I
| Entry DOI | 10.2210/pdb4p6i/pdb |
| Descriptor | CRISPR-associated endoribonuclease Cas2, CRISPR-associated endonuclease Cas1 (3 entities in total) |
| Functional Keywords | crispr-associated proteins, nuclease, hydrolase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 6 |
| Total formula weight | 156048.21 |
| Authors | Nunez, J.K.,Kranzusch, P.J.,Noeske, J.,Doudna, J.A. (deposition date: 2014-03-24, release date: 2014-05-07, Last modification date: 2023-12-27) |
| Primary citation | Nunez, J.K.,Kranzusch, P.J.,Noeske, J.,Wright, A.V.,Davies, C.W.,Doudna, J.A. Cas1-Cas2 complex formation mediates spacer acquisition during CRISPR-Cas adaptive immunity. Nat.Struct.Mol.Biol., 21:528-534, 2014 Cited by PubMed Abstract: The initial stage of CRISPR-Cas immunity involves the integration of foreign DNA spacer segments into the host genomic CRISPR locus. The nucleases Cas1 and Cas2 are the only proteins conserved among all CRISPR-Cas systems, yet the molecular functions of these proteins during immunity are unknown. Here we show that Cas1 and Cas2 from Escherichia coli form a stable complex that is essential for spacer acquisition and determine the 2.3-Å-resolution crystal structure of the Cas1-Cas2 complex. Mutations that perturb Cas1-Cas2 complex formation disrupt CRISPR DNA recognition and spacer acquisition in vivo. Active site mutants of Cas2, unlike those of Cas1, can still acquire new spacers, thus indicating a nonenzymatic role of Cas2 during immunity. These results reveal the universal roles of Cas1 and Cas2 and suggest a mechanism by which Cas1-Cas2 complexes specify sites of CRISPR spacer integration. PubMed: 24793649DOI: 10.1038/nsmb.2820 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
