Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for the non-self RNA-activated protease activity of the type III-E CRISPR nuclease-protease Craspase.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 7549, Year 2022
Publish date	Dec 7, 2022
Authors	Ning Cui / Jun-Tao Zhang / Zhuolin Li / Xiao-Yu Liu / Chongyuan Wang / Hongda Huang / Ning Jia /
PubMed Abstract	The RNA-targeting type III-E CRISPR-gRAMP effector interacts with a caspase-like protease TPR-CHAT to form the CRISPR-guided caspase complex (Craspase), but their functional mechanism is unknown. ...The RNA-targeting type III-E CRISPR-gRAMP effector interacts with a caspase-like protease TPR-CHAT to form the CRISPR-guided caspase complex (Craspase), but their functional mechanism is unknown. Here, we report cryo-EM structures of the type III-E gRAMP and gRAMP-TPR-CHAT complexes, before and after either self or non-self RNA target binding, and elucidate the mechanisms underlying RNA-targeting and non-self RNA-induced protease activation. The associated TPR-CHAT adopted a distinct conformation upon self versus non-self RNA target binding, with nucleotides at positions -1 and -2 of the CRISPR-derived RNA (crRNA) serving as a sensor. Only binding of the non-self RNA target activated the TPR-CHAT protease, leading to cleavage of Csx30 protein. Furthermore, TPR-CHAT structurally resembled eukaryotic separase, but with a distinct mechanism for protease regulation. Our findings should facilitate the development of gRAMP-based RNA manipulation tools, and advance our understanding of the virus-host discrimination process governed by a nuclease-protease Craspase during type III-E CRISPR-Cas immunity.
External links	Nat Commun / PubMed:36477448 / PubMed Central
Methods	EM (single particle)
Resolution	2.54 - 2.93 Å
Structure data	33676 7y80 EMDB-33676: CryoEM structure of type III-E CRISPR gRAMP-crRNA binary complex PDB-7y80: CryoEM structure of type III-E CRISPR Craspase gRAMP-crRNA binary complex Method: EM (single particle) / Resolution: 2.71 Å 33677 7y81 EMDB-33677: CryoEM structure of type III-E CRISPR gRAMP-crRNA complex bound to non-self RNA target PDB-7y81: CryoEM structure of type III-E CRISPR Craspase gRAMP-crRNA complex bound to non-self RNA target Method: EM (single particle) / Resolution: 2.54 Å 33678 7y82 EMDB-33678: CryoEM structure of type III-E CRISPR gRAMP-crRNA complex bound to self RNA target PDB-7y82: CryoEM structure of type III-E CRISPR Craspase gRAMP-crRNA complex bound to self RNA target Method: EM (single particle) / Resolution: 2.83 Å 33679 7y83 EMDB-33679: CryoEM structure of type III-E CRISPR gRAMP-crRNA in complex with TPR-CHAT bound to non-self RNA target PDB-7y83: CryoEM structure of type III-E CRISPR Craspase gRAMP-crRNA in complex with TPR-CHAT protease bound to non-self RNA target Method: EM (single particle) / Resolution: 2.93 Å 33680 7y84 EMDB-33680: CryoEM structure of type III-E CRISPR gRAMP-crRNA in complex with TPR-CHAT PDB-7y84: CryoEM structure of type III-E CRISPR Craspase gRAMP-crRNA in complex with TPR-CHAT protease Method: EM (single particle) / Resolution: 2.61 Å 33681 7y85 EMDB-33681: CryoEM structure of type III-E CRISPR gRAMP-crRNA in complex with TPR-CHAT bound to self RNA target PDB-7y85: CryoEM structure of type III-E CRISPR Craspase gRAMP-crRNA in complex with TPR-CHAT protease bound to self RNA target Method: EM (single particle) / Resolution: 2.73 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry
Source	candidatus scalindua brodae (bacteria)
Keywords	STRUCTURAL PROTEIN/RNA / Nuclease / STRUCTURAL PROTEIN-RNA COMPLEX / RNA BINDING PROTEIN