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8XX4

ASFV RNAP elongation complex

Summary for 8XX4
Entry DOI10.2210/pdb8xx4/pdb
EMDB information38745
DescriptorDNA-directed RNA polymerase subunit, RNA polymerase subunit 6, DNA (5'-D(P*CP*GP*CP*AP*AP*CP*GP*GP*CP*GP*A)-3'), ... (13 entities in total)
Functional Keywordsasfv, rnap, elongation complex, transcription/rna/dna, transcription-rna-dna complex
Biological sourceAfrican swine fever virus (ASFV)
More
Total number of polymer chains11
Total formula weight422746.28
Authors
Zhu, G.L.,Zhu, Y.,Zhu, Z.X.,Sun, F.,Zheng, H.X. (deposition date: 2024-01-17, release date: 2025-01-22)
Primary citationZhu, G.,Xi, F.,Zeng, W.,Zhao, Y.,Cao, W.,Liu, C.,Yang, F.,Ru, Y.,Xiao, S.,Zhang, S.,Liu, H.,Tian, H.,Yang, F.,Lu, B.,Sun, S.,Song, H.,Sun, B.,Zhao, X.,Tang, L.,Li, K.,He, J.,Guo, J.,Zhu, Y.,Zhu, Z.,Sun, F.,Zheng, H.
Structural basis of RNA polymerase complexes in African swine fever virus.
Nat Commun, 16:501-501, 2025
Cited by
PubMed Abstract: African swine fever virus is highly contagious and causes a fatal infectious disease in pigs, resulting in a significant global impact on pork supply. The African swine fever virus RNA polymerase serves as a crucial multifunctional protein complex responsible for genome transcription and regulation. Therefore, it is essential to investigate its structural and functional characteristics for the prevention and control of African swine fever. Here, we determine the structures of endogenous African swine fever virus RNA polymerase in both nucleic acid-free and elongation states. The African swine fever virus RNA polymerase shares similarities with the core of typical RNA polymerases, but possesses a distinct subunit M1249L. Notably, the dynamic binding mode of M1249L with RNA polymerase, along with the C-terminal tail insertion of M1249L in the active center of DNA-RNA scaffold binding, suggests the potential of M1249L to regulate RNA polymerase activity within cells. These results are important for understanding the transcription cycle of the African swine fever virus and for developing antiviral strategies.
PubMed: 39779680
DOI: 10.1038/s41467-024-55683-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.6 Å)
Structure validation

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