3JBX

Cryo-electron microscopy structure of RAG Signal End Complex (C2 symmetry)

3JBX の概要

• エントリーDOI: 10.2210/pdb3jbx/pdb
• 関連するPDBエントリー: 3JBW 3JBY
• EMDBエントリー: 6487 6488 6489 6490 6491
• 分子名称: V(D)J recombination-activating protein 1, V(D)J recombination-activating protein 2, 5'-D(*CP*AP*CP*AP*GP*TP*GP*CP*TP*AP*CP*AP*GP*AP*C)-3', ... (8 entities in total)
• 機能のキーワード: rag1, rag2, v(d)j recombination, signal end complex, antigen receptor gene recombination, t and b cell development, recombination-dna complex, recombination/dna
• 由来する生物種: Danio rerio (zebra fish); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 329947.30

構造登録者

Ru, H.,Chambers, M.G.,Fu, T.-M.,Tong, A.B.,Liao, M.,Wu, H. (登録日: 2015-10-22, 公開日: 2015-12-09, 最終更新日: 2024-02-21)

主引用文献

Ru, H.,Chambers, M.G.,Fu, T.M.,Tong, A.B.,Liao, M.,Wu, H.
Molecular Mechanism of V(D)J Recombination from Synaptic RAG1-RAG2 Complex Structures.
Cell(Cambridge,Mass.), 163:1138-1152, 2015

PubMed Abstract: Diverse repertoires of antigen-receptor genes that result from combinatorial splicing of coding segments by V(D)J recombination are hallmarks of vertebrate immunity. The (RAG1-RAG2)2 recombinase (RAG) recognizes recombination signal sequences (RSSs) containing a heptamer, a spacer of 12 or 23 base pairs, and a nonamer (12-RSS or 23-RSS) and introduces precise breaks at RSS-coding segment junctions. RAG forms synaptic complexes only with one 12-RSS and one 23-RSS, a dogma known as the 12/23 rule that governs the recombination fidelity. We report cryo-electron microscopy structures of synaptic RAG complexes at up to 3.4 Å resolution, which reveal a closed conformation with base flipping and base-specific recognition of RSSs. Distortion at RSS-coding segment junctions and base flipping in coding segments uncover the two-metal-ion catalytic mechanism. Induced asymmetry involving tilting of the nonamer-binding domain dimer of RAG1 upon binding of HMGB1-bent 12-RSS or 23-RSS underlies the molecular mechanism for the 12/23 rule.

PubMed: 26548953
DOI: 10.1016/j.cell.2015.10.055

実験手法

ELECTRON MICROSCOPY (3.4 Å)