8IQB

Crystal structure of AsfvPrimPol N-terminal Prim/Pol domain

Summary for 8IQB

• Entry DOI: 10.2210/pdb8iqb/pdb
• Descriptor: Putative primase C962R (2 entities in total)
• Functional Keywords: polymerase, primase, primpol, dna binding protein
• Biological source: African swine fever virus BA71V
• Total number of polymer chains: 2
• Total formula weight: 64547.45

Authors

Shao, Z.W.,Gan, J.H. (deposition date: 2023-03-16, release date: 2023-07-26, Last modification date: 2023-11-29)

Primary citation

Shao, Z.,Su, S.,Yang, J.,Zhang, W.,Gao, Y.,Zhao, X.,Zhang, Y.,Shao, Q.,Cao, C.,Li, H.,Liu, H.,Zhang, J.,Lin, J.,Ma, J.,Gan, J.
Structures and implications of the C962R protein of African swine fever virus.
Nucleic Acids Res., 51:9475-9490, 2023

PubMed Abstract: 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.

PubMed: 37587714
DOI: 10.1093/nar/gkad677

Experimental method

X-RAY DIFFRACTION (2.58 Å)