6ZXP

Solution structure of the C-terminal domain of the vaccinia virus DNA polymerase processivity factor component A20 fused to a short peptide from the viral DNA polymerase E9.

6ZXP の概要

• エントリーDOI: 10.2210/pdb6zxp/pdb
• NMR情報: BMRB: 34544
• 分子名称: DNA polymerase processivity factor component A20,DNA polymerase processivity factor component E9 (1 entity in total)
• 機能のキーワード: poxviridae, dna polymerase holoenzyme, processivity factor binding, replication
• 由来する生物種: Vaccinia virus Copenhagen; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16882.93

構造登録者

Bersch, B.,Tarbouriech, N.,Burmeister, W.,Iseni, F. (登録日: 2020-07-30, 公開日: 2021-05-19, 最終更新日: 2024-06-19)

主引用文献

Bersch, B.,Tarbouriech, N.,Burmeister, W.P.,Iseni, F.
Solution Structure of the C-terminal Domain of A20, the Missing Brick for the Characterization of the Interface between Vaccinia Virus DNA Polymerase and its Processivity Factor.
J.Mol.Biol., 433:167009-167009, 2021

PubMed Abstract: Poxviruses are enveloped viruses with a linear, double-stranded DNA genome. Viral DNA synthesis is achieved by a functional DNA polymerase holoenzyme composed of three essential proteins. For vaccinia virus (VACV) these are E9, the catalytic subunit, a family B DNA polymerase, and the heterodimeric processivity factor formed by D4 and A20. The A20 protein links D4 to the catalytic subunit. High-resolution structures have been obtained for the VACV D4 protein in complex with an N-terminal fragment of A20 as well as for E9. In addition, biochemical studies provided evidence that a poxvirus-specific insertion (insert 3) in E9 interacts with the C-terminal residues of A20. Here, we provide solution structures of two different VACV A20 C-terminal constructs containing residues 304-426, fused at their C-terminus to either a BAP (Biotin Acceptor Peptide)-tag or a short peptide containing the helix of E9 insert 3. Together with results from titration studies, these structures shed light on the molecular interface between the catalytic subunit and the processivity factor component A20. The interface comprises hydrophobic residues conserved within the Chordopoxvirinae subfamily. Finally, we constructed a HADDOCK model of the VACV A20-E9 complex, which is in excellent accordance with previous experimental data.

PubMed: 33901538
DOI: 10.1016/j.jmb.2021.167009

実験手法

SOLUTION NMR