4WWX

Crystal structure of the core RAG1/2 recombinase

Summary for 4WWX

• Entry DOI: 10.2210/pdb4wwx/pdb
• Descriptor: V(D)J recombination-activating protein 1, V(D)J recombination-activating protein 2, ZINC ION (3 entities in total)
• Functional Keywords: v(d)j recombination, rag1/2, recombination activating gene 1/2, crystal structure., hydrolase, ligase
• Biological source: Mus musculus (Mouse); More
• Cellular location: Nucleus : P15919 P21784
• Total number of polymer chains: 4
• Total formula weight: 219721.90

Authors

Kim, M.S.,Lapkouski, M.,Yang, W.,Gellert, M. (deposition date: 2014-11-12, release date: 2015-02-25, Last modification date: 2024-02-28)

Primary citation

Kim, M.S.,Lapkouski, M.,Yang, W.,Gellert, M.
Crystal structure of the V(D)J recombinase RAG1-RAG2.
Nature, 518:507-511, 2015

PubMed Abstract: V(D)J recombination in the vertebrate immune system generates a highly diverse population of immunoglobulins and T-cell receptors by combinatorial joining of segments of coding DNA. The RAG1-RAG2 protein complex initiates this site-specific recombination by cutting DNA at specific sites flanking the coding segments. Here we report the crystal structure of the mouse RAG1-RAG2 complex at 3.2 Å resolution. The 230-kilodalton RAG1-RAG2 heterotetramer is 'Y-shaped', with the amino-terminal domains of the two RAG1 chains forming an intertwined stalk. Each RAG1-RAG2 heterodimer composes one arm of the 'Y', with the active site in the middle and RAG2 at its tip. The RAG1-RAG2 structure rationalizes more than 60 mutations identified in immunodeficient patients, as well as a large body of genetic and biochemical data. The architectural similarity between RAG1 and the hairpin-forming transposases Hermes and Tn5 suggests the evolutionary conservation of these DNA rearrangements.

PubMed: 25707801
DOI: 10.1038/nature14174

Experimental method

X-RAY DIFFRACTION (3.2001 Å)