4MKY
Polymerase Domain from Mycobacterium tuberculosis Ligase D in complex with an annealed double-strand DNA break.
4MKY の概要
| エントリーDOI | 10.2210/pdb4mky/pdb |
| 関連するPDBエントリー | 2iru 2irx 2iry 2r9l 3pky |
| 分子名称 | DNA ligase-like protein Rv0938/MT0965, 5'-D(P*DGP*DCP*DGP*DGP*DC)-3', 5'-D(*DGP*DCP*DCP*DGP*DCP*DAP*DGP*DTP*DAP*DC)-3', ... (4 entities in total) |
| 機能のキーワード | protein-dna complex, transferase-dna complex, nucleotide-binding, polymerase, primase, transferase, transferase/dna |
| 由来する生物種 | Mycobacterium tuberculosis 詳細 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 149504.66 |
| 構造登録者 | |
| 主引用文献 | Brissett, N.C.,Martin, M.J.,Bartlett, E.J.,Bianchi, J.,Blanco, L.,Doherty, A.J. Molecular Basis for DNA Double-Strand Break Annealing and Primer Extension by an NHEJ DNA Polymerase. Cell Rep, 5:1108-1120, 2013 Cited by PubMed Abstract: Nonhomologous end-joining (NHEJ) is one of the major DNA double-strand break (DSB) repair pathways. The mechanisms by which breaks are competently brought together and extended during NHEJ is poorly understood. As polymerases extend DNA in a 5'-3' direction by nucleotide addition to a primer, it is unclear how NHEJ polymerases fill in break termini containing 3' overhangs that lack a primer strand. Here, we describe, at the molecular level, how prokaryotic NHEJ polymerases configure a primer-template substrate by annealing the 3' overhanging strands from opposing breaks, forming a gapped intermediate that can be extended in trans. We identify structural elements that facilitate docking of the 3' ends in the active sites of adjacent polymerases and reveal how the termini act as primers for extension of the annealed break, thus explaining how such DSBs are extended in trans. This study clarifies how polymerases couple break-synapsis to catalysis, providing a molecular mechanism to explain how primer extension is achieved on DNA breaks. PubMed: 24239356DOI: 10.1016/j.celrep.2013.10.016 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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