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2EWJ

Escherichia Coli Replication Terminator Protein (Tus) Complexed With DNA- Locked form

2EWJ の概要
エントリーDOI10.2210/pdb2ewj/pdb
関連するPDBエントリー1ECR
分子名称5'-D(*T*TP*AP*GP*TP*TP*AP*CP*AP*AP*CP*AP*TP*AP*CP*T)-3', 5'-D(*TP*G*AP*TP*AP*TP*GP*TP*TP*GP*TP*AP*AP*CP*TP*A)-3', DNA replication terminus site-binding protein, ... (5 entities in total)
機能のキーワードtus, terminus site, protein-dna interaction, replication arrest, replication-dna complex, replication/dna
由来する生物種Escherichia coli
細胞内の位置Cytoplasm: P16525
タンパク質・核酸の鎖数3
化学式量合計46007.32
構造登録者
Oakley, A.J.,Mulcair, M.D.,Schaeffer, P.M.,Dixon, N.E. (登録日: 2005-11-03, 公開日: 2006-05-03, 最終更新日: 2023-10-25)
主引用文献Mulcair, M.D.,Schaeffer, P.M.,Oakley, A.J.,Cross, H.F.,Neylon, C.,Hill, T.M.,Dixon, N.E.
A molecular mousetrap determines polarity of termination of DNA replication in E. coli.
Cell(Cambridge,Mass.), 125:1309-1319, 2006
Cited by
PubMed Abstract: During chromosome synthesis in Escherichia coli, replication forks are blocked by Tus bound Ter sites on approach from one direction but not the other. To study the basis of this polarity, we measured the rates of dissociation of Tus from forked TerB oligonucleotides, such as would be produced by the replicative DnaB helicase at both the fork-blocking (nonpermissive) and permissive ends of the Ter site. Strand separation of a few nucleotides at the permissive end was sufficient to force rapid dissociation of Tus to allow fork progression. In contrast, strand separation extending to and including the strictly conserved G-C(6) base pair at the nonpermissive end led to formation of a stable locked complex. Lock formation specifically requires the cytosine residue, C(6). The crystal structure of the locked complex showed that C(6) moves 14 A from its normal position to bind in a cytosine-specific pocket on the surface of Tus.
PubMed: 16814717
DOI: 10.1016/j.cell.2006.04.040
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 2ewj
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2025-12-31に公開中

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