3MTV

The Crystal Structure of the PRRSV Nonstructural Protein Nsp1

3MTV の概要

• エントリーDOI: 10.2210/pdb3mtv/pdb
• 分子名称: Papain-like cysteine protease (2 entities in total)
• 機能のキーワード: prrsv, nsp1, nuclease, papain-like cysteine protease, hydrolase
• 由来する生物種: Porcine reproductive and respiratory syndrome virus (PRRSV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23093.43

構造登録者

Xue, F.,Sun, Y.N.,Yan, L.M.,Zhao, C.,Lou, Z.Y.,Rao, Z.H. (登録日: 2010-04-30, 公開日: 2010-05-19, 最終更新日: 2024-03-20)

主引用文献

Xue, F.,Sun, Y.N.,Yan, L.M.,Zhao, C.,Chen, J.,Bartlam, M.,Li, X.M.,Lou, Z.Y.,Rao, Z.H.
The crystal structure of porcine reproductive and respiratory syndrome virus nonstructural protein Nsp1beta reveals a novel metal-dependent nuclease
J.Virol., 84:6461-6471, 2010

PubMed Abstract: Porcine reproductive and respiratory syndrome virus (PRRSV), a member of the Arteriviridae family of Nidovirales, is the causative agent of porcine reproductive and respiratory syndrome, which results in enormous economic losses in the swine industry. As the second protein encoded by the PRRSV genome, nsp1beta cleaves itself from the downstream nsp2 protein via a C-terminal papain-like cysteine protease (PCP) domain. Although nsp1beta is known to be involved in virulence, its precise role in the process of viral infection remains unclear. In this work, we describe the homodimeric crystal structure of PRRSV nsp1beta in its natural, self-processed form. We show that the architecture of its N-terminal domain (NTD) adopts a fold closely resembling that of several known nucleases and has intrinsic nuclease activity that is strongly activated by manganese ions in vitro. Key features, however, distinguish nsp1beta from characterized nucleases, including the C-terminal PCP domain (which is responsible for the self-release of nsp1beta from nsp2), a linker domain (LKD) that connects the NTD and the PCP domain, and a C-terminal extension (CTE) that binds to and is stabilized by the putative substrate binding site of the PCPbeta domain. Combined with the reported nuclear localization of this protein, these results shed light on the self-processing mode and precise biological function of nsp1beta and thus offer a multitarget template for future drug discovery.

PubMed: 20410261
DOI: 10.1128/JVI.00301-10

実験手法

X-RAY DIFFRACTION (2.8 Å)