2GDT

NMR Structure of the nonstructural protein 1 (nsp1) from the SARS coronavirus

2GDT の概要

• エントリーDOI: 10.2210/pdb2gdt/pdb
• NMR情報: BMRB: 7014
• 分子名称: Leader protein; p65 homolog; NSP1 (EC 3.4.22.-) (1 entity in total)
• 機能のキーワード: leader protein, beta-barrel, alpha-beta, virus, replicase, structural genomics, psi-2, protein structure initiative, joint center for structural genomics, jcsg, viral protein, hydrolase
• 由来する生物種: SARS coronavirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12680.53

構造登録者

Almeida, M.S.,Herrmann, T.,Geralt, M.,Johnson, M.A.,Saikatendu, K.,Joseph, J.,Subramanian, R.C.,Neuman, B.W.,Buchmeier, M.J.,Stevens, R.C.,Kuhn, P.,Wilson, I.A.,Wuthrich, K.,Joint Center for Structural Genomics (JCSG) (登録日: 2006-03-17, 公開日: 2007-02-06, 最終更新日: 2024-05-08)

主引用文献

Almeida, M.S.,Johnson, M.A.,Herrmann, T.,Geralt, M.,Wuthrich, K.
Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
J.Virol., 81:3151-3161, 2007

PubMed Abstract: The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome coronavirus has 179 residues and is the N-terminal cleavage product of the viral replicase polyprotein that mediates RNA replication and processing. The specific function of nsp1 is not known. Here we report the nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128, which represents a novel alpha/beta-fold formed by a mixed parallel/antiparallel six-stranded beta-barrel, an alpha-helix covering one opening of the barrel, and a 3(10)-helix alongside the barrel. We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered. The structure is analyzed in a search for possible correlations with the recently reported activity of nsp1 in the degradation of mRNA.

PubMed: 17202208
DOI: 10.1128/JVI.01939-06

実験手法

SOLUTION NMR