- PDB-8iqc: Crystal structure of AsfvPrimPol N-terminal Prim/Pol domain in co... -
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基本情報
登録情報
データベース: PDB / ID: 8iqc
タイトル
Crystal structure of AsfvPrimPol N-terminal Prim/Pol domain in complex with Mn2+
要素
Putative primase C962R
キーワード
DNA BINDING PROTEIN / polymerase / primase / PrimPol
機能・相同性
機能・相同性情報
hydrolase activity, acting on acid anhydrides / helicase activity / DNA replication / ATP binding / metal ion binding 類似検索 - 分子機能
Primase, C-terminal 2 / Primase C terminal 2 (PriCT-2) / Domain of unknown function DUF5906 / Family of unknown function (DUF5906) / Bacteriophage/plasmid primase, P4, C-terminal / D5 N terminal like / Helicase, superfamily 3, DNA virus / Superfamily 3 helicase of DNA viruses domain profile. / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
National Natural Science Foundation of China (NSFC)
中国
引用
ジャーナル: Nucleic Acids Res / 年: 2023 タイトル: Structures and implications of the C962R protein of African swine fever virus. 著者: Zhiwei Shao / Shichen Su / Jie Yang / Weizhen Zhang / Yanqing Gao / Xin Zhao / Yixi Zhang / Qiyuan Shao / Chulei Cao / Huili Li / Hehua Liu / Jinru Zhang / Jinzhong Lin / Jinbiao Ma / Jianhua Gan / 要旨: African swine fever virus (ASFV) is highly contagious and can cause lethal disease in pigs. Although it has been extensively studied in the past, no vaccine or other useful treatment against ASFV is ...African swine fever virus (ASFV) is highly contagious and can cause lethal disease in pigs. Although it has been extensively studied in the past, no vaccine or other useful treatment against ASFV is available. The genome of ASFV encodes more than 170 proteins, but the structures and functions for the majority of the proteins remain elusive, which hindered our understanding on the life cycle of ASFV and the development of ASFV-specific inhibitors. Here, we report the structural and biochemical studies of the highly conserved C962R protein of ASFV, showing that C962R is a multidomain protein. The N-terminal AEP domain is responsible for the DNA polymerization activity, whereas the DNA unwinding activity is catalyzed by the central SF3 helicase domain. The middle PriCT2 and D5_N domains and the C-terminal Tail domain all contribute to the DNA unwinding activity of C962R. C962R preferentially works on forked DNA, and likely functions in Base-excision repair (BER) or other repair pathway in ASFV. Although it is not essential for the replication of ASFV, C962R can serve as a model and provide mechanistic insight into the replicative primase proteins from many other species, such as nitratiruptor phage NrS-1, vaccinia virus (VACV) and other viruses.