EMD-37229
Structure of African swine fever virus topoisomerase II in complex with dsDNA
EMD-37229
Single-particle3.3 Å
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Map released: 03/04/2024
Last modified: 14/08/2024
Sample Organism:
African swine fever virus
Sample: pP1192R
Fitted models: 8kgp (Avg. Q-score: 0.529)
Deposition Authors: Cong J, Xin Y, Li X, Chen Y
Sample: pP1192R
Fitted models: 8kgp (Avg. Q-score: 0.529)
Deposition Authors: Cong J, Xin Y, Li X, Chen Y
Structural insights into the DNA topoisomerase II of the African swine fever virus.
Cong J,
Xin Y,
Kang H,
Yang Y,
Wang C,
Zhao D
,
Li X,
Rao Z,
Chen Y
(2024) Nat Commun , 15 , 4607 - 4607
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(2024) Nat Commun , 15 , 4607 - 4607
Abstract:
Type II topoisomerases are ubiquitous enzymes that play a pivotal role in modulating the topological configuration of double-stranded DNA. These topoisomerases are required for DNA metabolism and have been extensively studied in both prokaryotic and eukaryotic organisms. However, our understanding of virus-encoded type II topoisomerases remains limited. One intriguing example is the African swine fever virus, which stands as the sole mammalian-infecting virus encoding a type II topoisomerase. In this work, we use several approaches including cryo-EM, X-ray crystallography, and biochemical assays to investigate the structure and function of the African swine fever virus type II topoisomerase, pP1192R. We determine the structures of pP1192R in different conformational states and confirm its enzymatic activity in vitro. Collectively, our results illustrate the basic mechanisms of viral type II topoisomerases, increasing our understanding of these enzymes and presenting a potential avenue for intervention strategies to mitigate the impact of the African swine fever virus.
Type II topoisomerases are ubiquitous enzymes that play a pivotal role in modulating the topological configuration of double-stranded DNA. These topoisomerases are required for DNA metabolism and have been extensively studied in both prokaryotic and eukaryotic organisms. However, our understanding of virus-encoded type II topoisomerases remains limited. One intriguing example is the African swine fever virus, which stands as the sole mammalian-infecting virus encoding a type II topoisomerase. In this work, we use several approaches including cryo-EM, X-ray crystallography, and biochemical assays to investigate the structure and function of the African swine fever virus type II topoisomerase, pP1192R. We determine the structures of pP1192R in different conformational states and confirm its enzymatic activity in vitro. Collectively, our results illustrate the basic mechanisms of viral type II topoisomerases, increasing our understanding of these enzymes and presenting a potential avenue for intervention strategies to mitigate the impact of the African swine fever virus.