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Structure paper

TitleStructures and implications of the C962R protein of African swine fever virus.
Journal, issue, pagesNucleic Acids Res, Vol. 51, Issue 17, Page 9475-9490, Year 2023
Publish dateSep 22, 2023
AuthorsZhiwei Shao / Shichen Su / Jie Yang / Weizhen Zhang / Yanqing Gao / Xin Zhao / Yixi Zhang / Qiyuan Shao / Chulei Cao / Huili Li / Hehua Liu / Jinru Zhang / Jinzhong Lin / Jinbiao Ma / Jianhua Gan /
PubMed AbstractAfrican swine fever virus (ASFV) is highly contagious and can cause lethal disease in pigs. Although it has been extensively studied in the past, no vaccine or other useful treatment against ASFV is ...African swine fever virus (ASFV) is highly contagious and can cause lethal disease in pigs. Although it has been extensively studied in the past, no vaccine or other useful treatment against ASFV is available. The genome of ASFV encodes more than 170 proteins, but the structures and functions for the majority of the proteins remain elusive, which hindered our understanding on the life cycle of ASFV and the development of ASFV-specific inhibitors. Here, we report the structural and biochemical studies of the highly conserved C962R protein of ASFV, showing that C962R is a multidomain protein. The N-terminal AEP domain is responsible for the DNA polymerization activity, whereas the DNA unwinding activity is catalyzed by the central SF3 helicase domain. The middle PriCT2 and D5_N domains and the C-terminal Tail domain all contribute to the DNA unwinding activity of C962R. C962R preferentially works on forked DNA, and likely functions in Base-excision repair (BER) or other repair pathway in ASFV. Although it is not essential for the replication of ASFV, C962R can serve as a model and provide mechanistic insight into the replicative primase proteins from many other species, such as nitratiruptor phage NrS-1, vaccinia virus (VACV) and other viruses.
External linksNucleic Acids Res / PubMed:37587714 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2 - 3.67 Å
Structure data

35670

8iqh

EMDB-35670, PDB-8iqh:
Structure of Full-Length AsfvPrimPol in Apo-Form
Method: EM (single particle) / Resolution: 3.67 Å

35671

8iqi

EMDB-35671, PDB-8iqi:
Structure of Full-Length AsfvPrimPol in Complex-Form
Method: EM (single particle) / Resolution: 3.32 Å

PDB-8iqb:
Crystal structure of AsfvPrimPol N-terminal Prim/Pol domain
Method: X-RAY DIFFRACTION / Resolution: 2.58 Å

PDB-8iqc:
Crystal structure of AsfvPrimPol N-terminal Prim/Pol domain in complex with Mn2+
Method: X-RAY DIFFRACTION / Resolution: 2.0 Å

PDB-8iqd:
Crystal structure of AsfvPrimPol N-terminal Prim/Pol domain in complex with Mn2+ and dCTP
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MN:
Unknown entry

ChemComp-DCP:
2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • african swine fever virus ba71v
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / polymerase / primase / PrimPol / Helicase

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