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 of RNA-guided DNA integration by type I CRISPR-associated transposases.
Journal, issue, pages	bioRxiv, Year 2026
Publish date	May 18, 2026
Authors	Giada Finocchio / Seraina Oberli / George Lampe / Michael Schmitz / Samuel H Sternberg / Martin Jinek /
PubMed Abstract	CRISPR-associated transposases (CASTs) achieve site-specific DNA integration by coupling the RNA-guided targeting action of a nuclease-deficient CRISPR-Cas system with the assembly of a Tn7-like ...CRISPR-associated transposases (CASTs) achieve site-specific DNA integration by coupling the RNA-guided targeting action of a nuclease-deficient CRISPR-Cas system with the assembly of a Tn7-like transpososome complex. Understanding the detailed mechanisms of this elaborate process is paramount to engineering CAST systems into programmable genetic tools. The type I-F CAST (CAST) displays the highest activity in mammalian cells to date and has been the subject of extensive directed evolution, but efforts to rationally engineer further improvements have been hampered by critical gaps in our understanding of transpososome assembly and activation. Here we use cryo-EM structural analysis, validated by DNA transposition assays, to visualize the CAST system in a series of functional states that define the stepwise mechanism of RNA-guided DNA integration. The structure of a target DNA-bound Cascade-TniQ-TnsC complex reveals that conformational changes induced by R-loop formation are coupled to target DNA stabilization and TnsC heptamerization, which in turn recruits the TnsAB transposase via conserved interactions with its C-terminal tail. Finally, the structure of the 1.2 MDa CAST transpososome holocomplex reveals specific TnsC-TnsB and TnsB-target DNA interactions that drive allosteric remodelling of the TnsB catalytic site to activate donor DNA integration. Together, these findings establish a unified structural and mechanistic blueprint for RNA-guided DNA integration and lay the foundation for engineering next-generation DNA insertion systems for genome editing applications.
External links	bioRxiv / PubMed:42239233 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 3.4 Å
Structure data	EMDB-57728: TnsAB-focused cryo-EM volume of the PseCascade-TniQ-TnsC-TnsAB holocomplex Method: EM (single particle) / Resolution: 3.4 Å EMDB-57729: TnsC-focused cryo-EM volume of the PseCascade-TniQ-TnsC-TnsAB holocomplex Method: EM (single particle) / Resolution: 3.3 Å EMDB-57730: Cascade-TniQ-TnsC-focused cryo-EM volume of the PseCascade-TniQ-TnsC-TnsAB holocomplex Method: EM (single particle) / Resolution: 3.1 Å EMDB-57731: Consensus cryo-EM volume of the PseCascade-TniQ-TnsC-TnsAB holocomplex Method: EM (single particle) / Resolution: 3.1 Å 57736 30ga EMDB-57736, PDB-30ga: Cryo-EM structure of the PseCascade-TniQ-TnsC-TnsAB holocomplex Method: EM (single particle) / Resolution: 3.2 Å EMDB-57737: TnsC-focused cryo-EM volume of the PseCascade-TniQ-TnsC complex bound to TnsB-hook motifs Method: EM (single particle) / Resolution: 3.0 Å EMDB-57738: Consensus cryo-EM volume of the PseCascade-TniQ-TnsC complex bound to TnsB-hook motifs Method: EM (single particle) / Resolution: 2.8 Å 57739 30gb EMDB-57739, PDB-30gb: Cryo-EM structure of the PseCascade-TniQ-TnsC complex bound to PseTnsB-hook motifs Method: EM (single particle) / Resolution: 2.9 Å EMDB-57750: TnsC-focused cryo-EM volume of the PseCascade-TniQ-TnsC complex Method: EM (single particle) / Resolution: 3.4 Å EMDB-57751: Consensus cryo-EM volume of the PseCascade-TniQ-TnsC complex Method: EM (single particle) / Resolution: 3.1 Å EMDB-57757: Cryo-EM volume of the PseCascade-TniQ complex Method: EM (single particle) / Resolution: 3.2 Å EMDB-57758: Cryo-EM volume of the PseCascade complex Method: EM (single particle) / Resolution: 2.9 Å 57765 30gt EMDB-57765, PDB-30gt: Cryo-EM structure of the PseCascade-TniQ-TnsC complex Method: EM (single particle) / Resolution: 3.3 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM
Source	pseudoalteromonas sp. s983 (bacteria) escherichia coli k-12 (bacteria)
Keywords	DNA BINDING PROTEIN / Transposase / DNA-binding / RNA-binding / CRISPR-Cas / CRISPR-associated transposon