7N6I
ATP-bound TnsC-TniQ complex from ShCAST system
Summary for 7N6I
| Entry DOI | 10.2210/pdb7n6i/pdb |
| EMDB information | 23720 23721 23722 23723 23724 23725 23726 |
| Descriptor | TniQ (Homology model), TnsC, DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), ... (6 entities in total) |
| Functional Keywords | crispr, transposition, aaa+ atpase, tn7, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Scytonema hofmannii More |
| Total number of polymer chains | 12 |
| Total formula weight | 303705.70 |
| Authors | Park, J.,Tsai, A.W.L.,Mehrotra, E.,Kellogg, E.H. (deposition date: 2021-06-08, release date: 2021-07-28, Last modification date: 2024-05-29) |
| Primary citation | Park, J.U.,Tsai, A.W.,Mehrotra, E.,Petassi, M.T.,Hsieh, S.C.,Ke, A.,Peters, J.E.,Kellogg, E.H. Structural basis for target site selection in RNA-guided DNA transposition systems. Science, 373:768-774, 2021 Cited by PubMed Abstract: CRISPR-associated transposition systems allow guide RNA-directed integration of a single DNA cargo in one orientation at a fixed distance from a programmable target sequence. We used cryo-electron microscopy (cryo-EM) to define the mechanism that underlies this process by characterizing the transposition regulator, TnsC, from a type V-K CRISPR-transposase system. In this scenario, polymerization of adenosine triphosphate-bound TnsC helical filaments could explain how polarity information is passed to the transposase. TniQ caps the TnsC filament, representing a universal mechanism for target information transfer in Tn7/Tn7-like elements. Transposase-driven disassembly establishes delivery of the element only to unused protospacers. Finally, TnsC transitions to define the fixed point of insertion, as revealed by structures with the transition state mimic ADP•AlF These mechanistic findings provide the underpinnings for engineering CRISPR-associated transposition systems for research and therapeutic applications. PubMed: 34385391DOI: 10.1126/science.abi8976 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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