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7M99

ATPgS bound TnsC filament from ShCAST system

Summary for 7M99
Entry DOI10.2210/pdb7m99/pdb
EMDB information23720 23721 23722 23723 23724 23725 23726
DescriptorTnsC, DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3'), DNA (5'-D(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*A)-3'), ... (5 entities in total)
Functional Keywordscrispr, transposition, aaa+ atpase, tn7, dna binding protein-dna complex, dna binding protein/dna
Biological sourceScytonema hofmannii
More
Total number of polymer chains10
Total formula weight268265.28
Authors
Park, J.,Tsai, A.W.L.,Mehrotra, E.,Kellogg, E.H. (deposition date: 2021-03-30, release date: 2021-07-28, Last modification date: 2024-05-29)
Primary citationPark, 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: 34385391
DOI: 10.1126/science.abi8976
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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