Novel β-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus
Novel β-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus
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DOI：
10.1128/jvi.01939-06
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发表时间：
2007-04-01
影响因子：
5.4
通讯作者：
Wuthrich, Kurt
中科院分区：
文献类型：
--
作者：
Almeida, Marcius S.;Johnson, Margaret A.;Wuthrich, Kurt
严重急性呼吸综合征冠状病毒的非结构蛋白1（nsp 1）有179个残基，是介导RNA复制和加工的病毒复制酶多聚蛋白的N-末端切割产物。nsp 1的具体功能尚不清楚。在这里，我们报告的核磁共振结构的nsp 1片段从残基13至128，这代表了一个新的α/β折叠形成的混合平行/反平行六链β-桶，α-螺旋覆盖一个开口的桶，和3（10）-螺旋旁边的桶。我们进一步表征了全长179个残基的蛋白质，并表明残基1至12和129至179的多肽片段是灵活无序的。的结构进行了分析，在寻找可能的相关性与最近报道的活性nsp 1的mRNA的降解。
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.