8XXT

ASFV RNAP M1249L C-tail occupied complex2 (MCOC2)

8XXT の概要

• エントリーDOI: 10.2210/pdb8xxt/pdb
• EMDBエントリー: 38760
• 分子名称: DNA-directed RNA polymerase subunit, ZINC ION, MAGNESIUM ION, ... (11 entities in total)
• 機能のキーワード: asfv, rnap, m1249l c-tail occupied complex2 (mcoc2), transcription
• 由来する生物種: African swine fever virus (ASFV); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 578060.55

構造登録者

Zhu, G.L.,Zhu, Y.,Zhu, Z.X.,Sun, F.,Zheng, H.X. (登録日: 2024-01-19, 公開日: 2025-01-22, 最終更新日: 2025-07-16)

主引用文献

Zhu, 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

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

実験手法

ELECTRON MICROSCOPY (2.85 Å)