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From Proteopedia
ASFV RNAP M1249L C-tail occupied complex2 (MCOC2)
Structural highlights
FunctionA0A3S7XUW7_ASF Catalytic component of the DNA-directed RNA polymerase (RNAP) that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates (By similarity). Forms the polymerase active center together with RPB2 (By similarity). Part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template.[ARBA:ARBA00029401] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[RuleBase:RU004279] Publication Abstract from PubMedAfrican 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. Structural basis of RNA polymerase complexes in African swine fever virus.,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 Nat Commun. 2025 Jan 8;16(1):501. doi: 10.1038/s41467-024-55683-z. PMID:39779680[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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