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 activity of the type VII CRISPR-Cas system.
Journal, issue, pages	Nature, Vol. 633, Issue 8029, Page 465-472, Year 2024
Publish date	Aug 14, 2024
Authors	Jie Yang / Xuzichao Li / Qiuqiu He / Xiaoshen Wang / Jingjing Tang / Tongyao Wang / Yi Zhang / Feiyang Yu / Shuqin Zhang / Zhikun Liu / Lingling Zhang / Fumeng Liao / Hang Yin / Haiyan Zhao / Zengqin Deng / Heng Zhang /
PubMed Abstract	The newly identified type VII CRISPR-Cas candidate system uses a CRISPR RNA-guided ribonucleoprotein complex formed by Cas5 and Cas7 proteins to target RNA. However, the RNA cleavage is executed by a ...The newly identified type VII CRISPR-Cas candidate system uses a CRISPR RNA-guided ribonucleoprotein complex formed by Cas5 and Cas7 proteins to target RNA. However, the RNA cleavage is executed by a dedicated Cas14 nuclease, which is distinct from the effector nucleases of the other CRISPR-Cas systems. Here we report seven cryo-electron microscopy structures of the Cas14-bound interference complex at different functional states. Cas14, a tetrameric protein in solution, is recruited to the Cas5-Cas7 complex in a target RNA-dependent manner. The N-terminal catalytic domain of Cas14 binds a stretch of the substrate RNA for cleavage, whereas the C-terminal domain is primarily responsible for tethering Cas14 to the Cas5-Cas7 complex. The biochemical cleavage assays corroborate the captured functional conformations, revealing that Cas14 binds to different sites on the Cas5-Cas7 complex to execute individual cleavage events. Notably, a plugged-in arginine of Cas7 sandwiched by a C-shaped clamp of C-terminal domain precisely modulates Cas14 binding. More interestingly, target RNA cleavage is altered by a complementary protospacer flanking sequence at the 5' end, but not at the 3' end. Altogether, our study elucidates critical molecular details underlying the assembly of the interference complex and substrate cleavage in the type VII CRISPR-Cas system, which may help rational engineering of the type VII CRISPR-Cas system for biotechnological applications.
External links	Nature / PubMed:39143216
Methods	EM (single particle)
Resolution	2.85 - 3.2 Å
Structure data	39287 8yhd EMDB-39287, PDB-8yhd: Cryo-EM structure of CTR-bound type VII CRISPR-Cas complex at post-state I Method: EM (single particle) / Resolution: 2.93 Å 39288 8yhe EMDB-39288, PDB-8yhe: Cryo-EM structure of CTR-bound type VII CRISPR-Cas complex at post-state II Method: EM (single particle) / Resolution: 3.07 Å 39766 8z4j EMDB-39766, PDB-8z4j: Cryo-EM structure of CTR-bound type VII CRISPR-Cas complex at substrate-engaged state II Method: EM (single particle) / Resolution: 2.97 Å 39767 8z4l EMDB-39767, PDB-8z4l: Cryo-EM structure of CTR-bound type VII CRISPR-Cas complex at substrate-engaged state I Method: EM (single particle) / Resolution: 2.85 Å 39857 8z99 EMDB-39857, PDB-8z99: Cryo-EM structure of NTR-bound type VII CRISPR-Cas complex at substrate-engaged state +I Method: EM (single particle) / Resolution: 3.2 Å 39859 8z9c EMDB-39859, PDB-8z9c: Cryo-EM structure of NTR-bound type VII CRISPR-Cas complex at substrate-engaged state I Method: EM (single particle) / Resolution: 3.01 Å 39861 8z9e EMDB-39861, PDB-8z9e: Cryo-EM structure of NTR-bound type VII CRISPR-Cas complex at substrate-engaged state II Method: EM (single particle) / Resolution: 3.13 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	metagenome (others)
Keywords	ANTIVIRAL PROTEIN / a protein complex / protein structure