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Structure paper

TitleStructural basis of RNA polymerase complexes in African swine fever virus.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 501, Year 2025
Publish dateJan 8, 2025
AuthorsGuoliang Zhu / Fei Xi / Wuxia Zeng / Yifei Zhao / Weijun Cao / Chen Liu / Fan Yang / Yi Ru / Shuqi Xiao / Shilei Zhang / Huanan Liu / Hong Tian / Fayu Yang / Biao Lu / Shukai Sun / Haiyang Song / Bozhang Sun / Xiaoyi Zhao / Lijie Tang / Kangli Li / Jijun He / Jianhong Guo / Yun Zhu / Zixiang Zhu / Fei Sun / Haixue Zheng /
PubMed AbstractAfrican 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 ...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.
External linksNat Commun / PubMed:39779680 / PubMed Central
MethodsEM (single particle)
Resolution2.4 - 3.0 Å
Structure data

38745

8xx4

EMDB-38745, PDB-8xx4:
ASFV RNAP elongation complex
Method: EM (single particle) / Resolution: 2.6 Å

38746

8xx5

EMDB-38746, PDB-8xx5:
ASFV RNAP M1249L C-tail occupied complex1 (MCOC1)
Method: EM (single particle) / Resolution: 2.4 Å

38757

8xxp

EMDB-38757, PDB-8xxp:
ASFV RNAP core complex
Method: EM (single particle) / Resolution: 2.6 Å

38760

8xxt

EMDB-38760, PDB-8xxt:
ASFV RNAP M1249L C-tail occupied complex2 (MCOC2)
Method: EM (single particle) / Resolution: 2.85 Å

38767

8xy6

EMDB-38767, PDB-8xy6:
ASFV RNAP M1249L C-tail occupied complex3 (MCOC3)
Method: EM (single particle) / Resolution: 3.0 Å

38802

8y0e

EMDB-38802, PDB-8y0e:
ASFV RNAP M1249L C-tail occupied complex4 (MCOC4)
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • african swine fever virus
KeywordsTRANSCRIPTION/RNA/DNA / ASFV / RNAP / elongation complex / TRANSCRIPTION-RNA-DNA complex / TRANSCRIPTION / M1249L C-tail occupied complex1 (MCOC1) / core complex / M1249L C-tail occupied complex2 (MCOC2) / M1249L C-tail occupied complex3 (MCOC3) / M1249L C-tail occupied complex4 (MCOC4)

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