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首页> 外文期刊>Journal of Molecular Biology >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
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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

机译：A20的C末端域的溶液结构，缺失砖的表征疫苗病毒DNA聚合酶与其加工系数之间的界面

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摘要

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(304-426)-E9 complex, which is in excellent accordance with previous experimental data. (C) 2021 Elsevier Ltd. All rights reserved.
机译：痘病毒是具有线性双链DNA基因组的包膜病毒。病毒DNA合成是通过一种由三种必需蛋白质组成的功能性DNA聚合酶全酶实现的。对于痘苗病毒（VACV），它们是E9，催化亚单位，B族DNA聚合酶，以及由D4和A20形成的异二聚体过程性因子。A20蛋白将D4连接到催化亚单位。VACV D4蛋白与A20的N末端片段以及E9的复合物已获得高分辨率结构。此外，生化研究提供了证据，证明E9中的痘病毒特异性插入（插入3）与A20的C末端残基相互作用。在这里，我们提供了两种不同的VACV A20 C端结构的溶液结构，其中含有残基304-426，在其C端与BAP（生物素受体肽）标签或含有E9插入3螺旋的短肽融合。结合滴定研究的结果，这些结构揭示了催化亚基和加工因子组分A20之间的分子界面。该界面包含保存在Chordopoxvirinae亚家族内的疏水残基。最后，我们构建了VACV A20（304-426）-E9复合物的黑线鳕模型，该模型与之前的实验数据非常吻合。（c）2021爱思唯尔有限公司保留所有权利。

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