4F3M
Crystal structure of CRISPR-associated protein
Summary for 4F3M
Entry DOI | 10.2210/pdb4f3m/pdb |
Descriptor | BH0337 protein, 1,2-ETHANEDIOL, SULFATE ION, ... (4 entities in total) |
Functional Keywords | crispr, ferredoxin fold, endoribonuclease, rna, rna binding protein |
Biological source | Bacillus halodurans |
Total number of polymer chains | 2 |
Total formula weight | 54711.70 |
Authors | |
Primary citation | Nam, K.H.,Haitjema, C.,Liu, X.,Ding, F.,Wang, H.,Delisa, M.P.,Ke, A. Cas5d Protein Processes Pre-crRNA and Assembles into a Cascade-like Interference Complex in Subtype I-C/Dvulg CRISPR-Cas System. Structure, 20:1574-1584, 2012 Cited by PubMed Abstract: Clustered regularly interspaced short palindromic repeats (CRISPRs), together with an operon of CRISPR-associated (Cas) proteins, form an RNA-based prokaryotic immune system against exogenous genetic elements. Cas5 family proteins are found in several type I CRISPR-Cas systems. Here, we report the molecular function of subtype I-C/Dvulg Cas5d from Bacillus halodurans. We show that Cas5d cleaves pre-crRNA into unit length by recognizing both the hairpin structure and the 3' single stranded sequence in the CRISPR repeat region. Cas5d structure reveals a ferredoxin domain-based architecture and a catalytic triad formed by Y46, K116, and H117 residues. We further show that after pre-crRNA processing, Cas5d assembles with crRNA, Csd1, and Csd2 proteins to form a multi-sub-unit interference complex similar to Escherichia coli Cascade (CRISPR-associated complex for antiviral defense) in architecture. Our results suggest that formation of a crRNA-presenting Cascade-like complex is likely a common theme among type I CRISPR subtypes. PubMed: 22841292DOI: 10.1016/j.str.2012.06.016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.71 Å) |
Structure validation
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