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2R9L

Polymerase Domain from Mycobacterium tuberculosis Ligase D in complex with DNA

2R9L の概要
エントリーDOI10.2210/pdb2r9l/pdb
関連するPDBエントリー2IRU 2IRX 2IRY
分子名称DNA (5'-D(P*DGP*DCP*DGP*DGP*DC)-3'), DNA (5'-D(*DGP*DCP*DCP*DGP*DCP*DAP*DAP*DCP*DGP*DCP*DA)-3'), DNA (5'-D(*DGP*DCP*DCP*DGP*DCP*DAP*DAP*DCP*DGP*DCP*DAP*DCP*DG)-3'), ... (7 entities in total)
機能のキーワードtransferase, protein-dna complex, atp-binding, ligase, nucleotide-binding, transferase-dna complex, transferase/dna
由来する生物種Mycobacterium tuberculosis H37Rv
詳細
タンパク質・核酸の鎖数6
化学式量合計76445.64
構造登録者
Brissett, N.C.,Fox, G.C.,Pitcher, R.S.,Doherty, A.J. (登録日: 2007-09-13, 公開日: 2008-01-08, 最終更新日: 2023-08-30)
主引用文献Brissett, N.C.,Pitcher, R.S.,Juarez, R.,Picher, A.J.,Green, A.J.,Dafforn, T.R.,Fox, G.C.,Blanco, L.,Doherty, A.J.
Structure of a NHEJ polymerase-mediated DNA synaptic complex
Science, 318:456-459, 2007
Cited by
PubMed Abstract: Nonhomologous end joining (NHEJ) is a critical DNA double-strand break (DSB) repair pathway required to maintain genome stability. Many prokaryotes possess a minimalist NHEJ apparatus required to repair DSBs during stationary phase, composed of two conserved core proteins, Ku and ligase D (LigD). The crystal structure of Mycobacterium tuberculosis polymerase domain of LigD mediating the synapsis of two noncomplementary DNA ends revealed a variety of interactions, including microhomology base pairing, mismatched and flipped-out bases, and 3' termini forming hairpin-like ends. Biochemical and biophysical studies confirmed that polymerase-induced end synapsis also occurs in solution. We propose that this DNA synaptic structure reflects an intermediate bridging stage of the NHEJ process, before end processing and ligation, with both the polymerase and the DNA sequence playing pivotal roles in determining the sequential order of synapsis and remodeling before end joining.
PubMed: 17947582
DOI: 10.1126/science.1145112
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 2r9l
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2026-04-22に公開中

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