8HG1
The structure of MPXV polymerase holoenzyme in replicating state
8HG1 の概要
エントリーDOI | 10.2210/pdb8hg1/pdb |
EMDBエントリー | 34731 |
分子名称 | DNA polymerase, E4R, DNA polymerase processivity factor component A20, ... (7 entities in total) |
機能のキーワード | mpxv, polymerase, replication, replication-dna complex, replication/dna |
由来する生物種 | Monkeypox virus (monkeypox) 詳細 |
タンパク質・核酸の鎖数 | 5 |
化学式量合計 | 214116.73 |
構造登録者 | |
主引用文献 | Peng, Q.,Xie, Y.,Kuai, L.,Wang, H.,Qi, J.,Gao, G.F.,Shi, Y. Structure of monkeypox virus DNA polymerase holoenzyme. Science, 379:100-105, 2023 Cited by PubMed Abstract: The World Health Organization declared mpox (or monkeypox) a public health emergency of international concern in July 2022, and prophylactic and therapeutic measures are in urgent need. The monkeypox virus (MPXV) has its own DNA polymerase F8, together with the processive cofactors A22 and E4, constituting the polymerase holoenzyme for genome replication. Here, we determined the holoenzyme structure in complex with DNA using cryo-electron microscopy at the global resolution of ~2.8 angstroms. The holoenzyme possesses an architecture that suggests a "forward sliding clamp" processivity mechanism for viral DNA replication. MPXV polymerase has a DNA binding mode similar to that of other B-family DNA polymerases from different species. These findings reveal the mechanism of the MPXV genome replication and may guide the development of anti-poxvirus drugs. PubMed: 36520947DOI: 10.1126/science.ade6360 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.8 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
