7Y57

Crystal structure of NS1 nuclease domain in P21 space group

7Y57 の概要

• エントリーDOI: 10.2210/pdb7y57/pdb
• 分子名称: NS1 protein, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: ns1, nuclease domain, dna binding protein
• 由来する生物種: Human parvovirus B19 (HPV B19)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 40089.86

構造登録者

Zhang, X.Y.,Gan, J.H. (登録日: 2022-06-16, 公開日: 2023-07-05, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.183 Å)