Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8KGT

Structure of African swine fever virus topoisomerase II in complex with dsDNA

Summary for 8KGT
Entry DOI10.2210/pdb8kgt/pdb
DescriptorDNA topoisomerase 2, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordstopo 2, viral protein
Biological sourceAfrican swine fever virus
Total number of polymer chains1
Total formula weight49946.25
Authors
Cong, J.,Xin, Y.,Li, X.,Chen, Y. (deposition date: 2023-08-19, release date: 2024-04-03, Last modification date: 2024-08-14)
Primary citationCong, J.,Xin, Y.,Kang, H.,Yang, Y.,Wang, C.,Zhao, D.,Li, X.,Rao, Z.,Chen, Y.
Structural insights into the DNA topoisomerase II of the African swine fever virus.
Nat Commun, 15:4607-4607, 2024
Cited by
PubMed 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.
PubMed: 38816407
DOI: 10.1038/s41467-024-49047-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

227344

數據於2024-11-13公開中

PDB statisticsPDBj update infoContact PDBjnumon