2gdt

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

Overview

The nonstructural protein 1 (nsp1) of the SARS coronavirus (CoV) 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 NMR structure of, nsp1(13-128), which represents a novel alpha/beta-fold formed by a mixed, parallel/antiparallel 6-stranded beta-barrel, an alpha-helix covering one, opening of the barrel, and a 310-helix alongside the barrel. We further, characterized the full-length 179-residue protein and show that the, polypeptide segments of residues 1-12 and 129-179 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.

About this Structure

2GDT is a Single protein structure of sequence from Sars coronavirus. Full crystallographic information is available from OCA.

Reference

Novel {beta}-barrel Fold in the NMR Structure of the Replicase Nonstructural Protein 1 from the SARS Coronavirus., Almeida MS, Johnson MA, Herrmann T, Geralt M, Wuthrich K, J Virol. 2007 Jan 3;. PMID:17202208

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