30jv

Cryo-EM structure of the PseTnsAB paired-end complex (right end) in the presence of Mn

spinqualitylabelsall models 30jv, resolution 2.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 30jv is a 8 chain structure with sequence from Pseudoalteromonas sp. S983. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.86Å Ligands: MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed CRISPR-associated transposons (CASTs) are Tn7-like elements that have co-opted RNA-guided CRISPR effectors for targeted DNA insertion. CASTs have been adapted as genome editing tools for programmable, site-specific integration. Among them, the type I-F system from Ps e udoalteromonas ( Pse CAST) shows uniquely robust activity in human cells, yet its mechanistic basis remains poorly understood. Here, we present structural and biochemical analysis of the Pse CAST transposase TnsAB. Biochemical reconstitution of transposon DNA excision defines key characteristics of the transposition mechanism. Cryogenic electron microscopy (cryo-EM) structures of Pse TnsAB paired-end complexes reveal molecular determinants of transpososome assembly, transposon end recognition and cleavage. We validate these findings using biochemical and in vivo assays of structure-based transposase mutants, and provide mechanistic insights into the enhanced activity of a laboratory-evolved TnsAB variant. Together, our studies highlight molecular features underlying the efficiency of natural and engineered type I-F transposases and establish a mechanistic framework for their continued rational optimization. Transposon end recognition and excision mechanisms of type I-F CRISPR-associated transposases.,Walter M, Finocchio G, Oberli S, Hammerschmid IC, Lampe GD, Karan J, Swartjes T, Sternberg SH, Jinek M, Querques I bioRxiv [Preprint]. 2026 May 7:2026.05.05.722991. doi: , 10.64898/2026.05.05.722991. PMID:42146515 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA