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5N2E

Structure of the E9 DNA polymerase from vaccinia virus

5N2E の概要
エントリーDOI10.2210/pdb5n2e/pdb
分子名称DNA polymerase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLYCEROL, ... (6 entities in total)
機能のキーワードvaccinia virus, dna polymerase, protein-protein interface, family b polymerase, processivity factor, transferase
由来する生物種Vaccinia virus (strain Copenhagen) (VACV)
タンパク質・核酸の鎖数1
化学式量合計118549.77
構造登録者
Tarbouriech, N.,Burmeister, W.P.,Iseni, F. (登録日: 2017-02-07, 公開日: 2017-11-29, 最終更新日: 2024-05-08)
主引用文献Tarbouriech, N.,Ducournau, C.,Hutin, S.,Mas, P.J.,Man, P.,Forest, E.,Hart, D.J.,Peyrefitte, C.N.,Burmeister, W.P.,Iseni, F.
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.
Nat Commun, 8:1455-1455, 2017
Cited by
PubMed Abstract: Vaccinia virus (VACV), the prototype member of the Poxviridae, replicates in the cytoplasm of an infected cell. The catalytic subunit of the DNA polymerase E9 binds the heterodimeric processivity factor A20/D4 to form the functional polymerase holoenzyme. Here we present the crystal structure of full-length E9 at 2.7 Å resolution that permits identification of important poxvirus-specific structural insertions. One insertion in the palm domain interacts with C-terminal residues of A20 and thus serves as the processivity factor-binding site. This is in strong contrast to all other family B polymerases that bind their co-factors at the C terminus of the thumb domain. The VACV E9 structure also permits rationalization of polymerase inhibitor resistance mutations when compared with the closely related eukaryotic polymerase delta-DNA complex.
PubMed: 29129932
DOI: 10.1038/s41467-017-01542-z
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.74 Å)
構造検証レポート
Validation report summary of 5n2e
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2024-10-30に公開中

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