6SA1
Post catalytic complex of Prim-PolC from Mycobacterium smegmatis with gapped DNA and 3'-dUTP
6SA1 の概要
エントリーDOI | 10.2210/pdb6sa1/pdb |
分子名称 | DNA polymerase LigD, polymerase domain, PYROPHOSPHATE, DNA (5'-D(P*GP*CP*GP*AP*GP*CP*G)-3'), ... (11 entities in total) |
機能のキーワード | nucleotidyl transferase, polymerase, base excision repair, transferase, protein-dna complex |
由来する生物種 | Mycolicibacterium smegmatis MC2 155 詳細 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 98237.70 |
構造登録者 | |
主引用文献 | Brissett, N.C.,Zabrady, K.,Plocinski, P.,Bianchi, J.,Korycka-Machala, M.,Brzostek, A.,Dziadek, J.,Doherty, A.J. Molecular basis for DNA repair synthesis on short gaps by mycobacterial Primase-Polymerase C. Nat Commun, 11:4196-4196, 2020 Cited by PubMed Abstract: Cells utilise specialized polymerases from the Primase-Polymerase (Prim-Pol) superfamily to maintain genome stability. Prim-Pol's function in genome maintenance pathways including replication, repair and damage tolerance. Mycobacteria contain multiple Prim-Pols required for lesion repair, including Prim-PolC that performs short gap repair synthesis during excision repair. To understand the molecular basis of Prim-PolC's gap recognition and synthesis activities, we elucidated crystal structures of pre- and post-catalytic complexes bound to gapped DNA substrates. These intermediates explain its binding preference for short gaps and reveal a distinctive modus operandi called Synthesis-dependent Template Displacement (STD). This mechanism enables Prim-PolC to couple primer extension with template base dislocation, ensuring that the unpaired templating bases in the gap are ushered into the active site in an ordered manner. Insights provided by these structures establishes the molecular basis of Prim-PolC's gap recognition and extension activities, while also illuminating the mechanisms of primer extension utilised by closely related Prim-Pols. PubMed: 32826907DOI: 10.1038/s41467-020-18012-8 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.01 Å) |
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