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2Z43

Structure of a twinned crystal of RadA

2Z43 の概要
エントリーDOI10.2210/pdb2z43/pdb
関連するPDBエントリー2dfl
分子名称DNA repair and recombination protein radA (2 entities in total)
機能のキーワードarchaea, filament, dna binding, recombination, molecular switch, reca, rad51, dmc1
由来する生物種Sulfolobus solfataricus
タンパク質・核酸の鎖数3
化学式量合計107742.09
構造登録者
Chen, L.T.,Ko, T.P.,Wang, A.H.J.,Wang, T.F. (登録日: 2007-06-12, 公開日: 2007-11-13, 最終更新日: 2023-11-01)
主引用文献Chen, L.T.,Ko, T.P.,Chang, Y.W.,Lin, K.A.,Wang, A.H.J.,Wang, T.F.
Structural and functional analyses of five conserved positively charged residues in the L1 and N-terminal DNA binding motifs of archaeal RADA protein
Plos One, 2:e858-e858, 2007
Cited by
PubMed Abstract: RecA family proteins engage in an ATP-dependent DNA strand exchange reaction that includes a ssDNA nucleoprotein helical filament and a homologous dsDNA sequence. In spite of more than 20 years of efforts, the molecular mechanism of homology pairing and strand exchange is still not fully understood. Here we report a crystal structure of Sulfolobus solfataricus RadA overwound right-handed filament with three monomers per helical pitch. This structure reveals conformational details of the first ssDNA binding disordered loop (denoted L1 motif) and the dsDNA binding N-terminal domain (NTD). L1 and NTD together form an outwardly open palm structure on the outer surface of the helical filament. Inside this palm structure, five conserved basic amino acid residues (K27, K60, R117, R223 and R229) surround a 25 A pocket that is wide enough to accommodate anionic ssDNA, dsDNA or both. Biochemical analyses demonstrate that these five positively charged residues are essential for DNA binding and for RadA-catalyzed D-loop formation. We suggest that the overwound right-handed RadA filament represents a functional conformation in the homology search and pairing reaction. A new structural model is proposed for the homologous interactions between a RadA-ssDNA nucleoprotein filament and its dsDNA target.
PubMed: 17848989
DOI: 10.1371/journal.pone.0000858
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.93 Å)
構造検証レポート
Validation report summary of 2z43
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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