Cryo-EM structure of mouse RAG1/2 PRC complex (DNA1)
Year: 2019
Type: dataset
Abstract: A single enzyme active site that catalyzes multiple reactions is a well-established biochemical theme, but how one nuclease site cleaves both DNA strands of a double helix has not been well understood. In analyzing site-specific DNA cleavage by the mammalian RAG1-RAG2 recombinase, which initiates V(D)J recombination, we find that the active site is reconfigured for the two consecutive reactions and the DNA double helix adopts drastically different structures. For initial nicking of the DNA, a locally unwound and unpaired DNA duplex forms a zipper via alternating interstrand base stacking, rather than melting as generally thought. The second strand cleavage and formation of a hairpin-DNA product requires a global scissor-like movement of protein and DNA, delivering the scissile phosphate into the rearranged active site.
Source: Worldwide Protein Data Bank
DOI: 10.2210/pdb6oen/pdb
Authors: X. Chen, Y. Cui, Z.H. Zhou, W. Yang, M. Gellert
Language: English
Topic: DNA Repair Mechanisms
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Awards: Structural and mechanistic studies of V(D)J recombination, Direct Detection Device for atomic resolution cryoEM of macromolecular complexes, Structural and mechanistic studies Of DNA mismatch repair, West/Midwest Consortium for High-Resolution Cryo Electron Microscopy, Structural and mechanistic studies of RNase H and HIV reverse transcriptase, High-End CryoEM Instrument for the UCLA Electron Imaging Center for Nanomachines, Structural studies of the post-cleavage complex in V(D)J recombination, Structural studies of proteins involved in DNA repair and recombination, High-Resolution CryoEM Reconstruction of Large Complexes
OpenAlex ID: W3003465770