6OER

Cryo-EM structure of mouse RAG1/2 NFC complex (DNA2)

Summary for 6OER

• Entry DOI: 10.2210/pdb6oer/pdb
• Related: 6OEM 6OEN 6OEO 6OEP 6OEQ
• EMDB information: 20030 20031 20032 20033 20034 20035
• Descriptor: V(D)J recombination-activating protein 1, V(D)J recombination-activating protein 2, DNA (46-MER), ... (9 entities in total)
• Functional Keywords: v(d)j recombination, dna transposition, rag, scid, recombination, recombination-dna complex, recombination/dna
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 9
• Total formula weight: 444598.37

Authors

Chen, X.,Cui, Y.,Zhou, Z.H.,Yang, W.,Gellert, M. (deposition date: 2019-03-27, release date: 2020-01-29, Last modification date: 2024-03-20)

Primary citation

Chen, X.,Cui, Y.,Best, R.B.,Wang, H.,Zhou, Z.H.,Yang, W.,Gellert, M.
Cutting antiparallel DNA strands in a single active site.
Nat.Struct.Mol.Biol., 27:119-126, 2020

PubMed 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.

PubMed: 32015552
DOI: 10.1038/s41594-019-0363-2

Experimental method

ELECTRON MICROSCOPY (3.29 Å)