8GNA
Structure of the SbCas7-11-crRNA-NTR complex
Summary for 8GNA
Entry DOI | 10.2210/pdb8gna/pdb |
EMDB information | 34158 |
Descriptor | RAMP superfamily protein, RNA (32-MER), RNA (5'-R(P*GP*GP*GP*GP*CP*AP*GP*AP*AP*AP*AP*UP*UP*GP*GP*GP*U)-3'), ... (4 entities in total) |
Functional Keywords | complex, rna-binding, rna binding protein |
Biological source | Candidatus Scalindua brodae More |
Total number of polymer chains | 3 |
Total formula weight | 222409.64 |
Authors | |
Primary citation | Wang, X.,Yu, G.,Wen, Y.,An, Q.,Li, X.,Liao, F.,Lian, C.,Zhang, K.,Yin, H.,Wei, Y.,Deng, Z.,Zhang, H. Target RNA-guided protease activity in type III-E CRISPR-Cas system. Nucleic Acids Res., 50:12913-12923, 2022 Cited by PubMed Abstract: The type III-E CRISPR-Cas systems are newly identified adaptive immune systems in prokaryotes that use a single Cas7-11 protein to specifically cleave target RNA. Cas7-11 could associate with Csx29, a putative caspase-like protein encoded by the gene frequently found in the type III-E loci, suggesting a functional linkage between the RNase and protease activities in type III-E systems. Here, we demonstrated that target RNA recognition would stimulate the proteolytic activity of Csx29, and protein Csx30 is the endogenous substrate. More interestingly, while the cognate target RNA recognition would activate Csx29, non-cognate target RNA with the complementary 3' anti-tag sequence inhibits the enzymatic activity. Csx30 could bind to the sigma factor RpoE, which may initiate the stress response after proteolytic cleavage. Combined with biochemical and structural studies, we have elucidated the mechanisms underlying the target RNA-guided proteolytic activity of Csx29. Our work will guide further developments leveraging this simple RNA targeting system for RNA and protein-related applications. PubMed: 36484100DOI: 10.1093/nar/gkac1151 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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