7Y57

Crystal structure of NS1 nuclease domain in P21 space group

Summary for 7Y57

• Entry DOI: 10.2210/pdb7y57/pdb
• Descriptor: NS1 protein, PHOSPHATE ION (3 entities in total)
• Functional Keywords: ns1, nuclease domain, dna binding protein
• Biological source: Human parvovirus B19 (HPV B19)
• Total number of polymer chains: 2
• Total formula weight: 40089.86

Authors

Zhang, X.Y.,Gan, J.H. (deposition date: 2022-06-16, release date: 2023-07-05, Last modification date: 2024-10-16)

Primary citation

Zhang, Y.,Shao, Z.,Gao, Y.,Fan, B.,Yang, J.,Chen, X.,Zhao, X.,Shao, Q.,Zhang, W.,Cao, C.,Liu, H.,Gan, J.
Structures and implications of the nuclease domain of human parvovirus B19 NS1 protein.
Comput Struct Biotechnol J, 20:4645-4655, 2022

PubMed Abstract: Infection of human parvovirus B19 (B19V) can cause a variety of diseases, such as hydrops fetalis, erythema infectiosum in children and acute arthropathy in women. Although B19V infection mainly occurs during childhood, about 50 % of adults are still susceptible to B19V infection. As the major replication protein of B19V, deletion of NS1 completely abolishes the infectivity of the virus. The nuclease domain of NS1 (NS1_Nuc) is responsible for DNA Ori binding and nicking that is critical for B19V viral DNA replication. NS1 has various variants, the structure and function for the majority of the variants are poorly studied. Here, we report two high-resolution crystal structures of NS1_Nuc, revealed the detailed conformations of many key residues. Structural comparison indicates that these residues are important for ssDNA or dsDNA binding by NS1. NS1 belongs to the HUH-endonuclease superfamily and it shares conserved ssDNA cleavage mechanism with other HUH-endonuclease members. However, our structural analyses, mutagenesis and assay results all suggested that NS1_Nuc utilizes one unique model in ssDNA binding.

PubMed: 36090819
DOI: 10.1016/j.csbj.2022.08.047

Experimental method

X-RAY DIFFRACTION (2.183 Å)