2fyg

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2fyg, resolution 1.80Å

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Crystal structure of NSP10 from Sars coronavirus

Overview

The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a, large 29.7-kb positive-stranded RNA genome. The first open reading frame, encodes replicase polyproteins 1a and 1ab, which are cleaved to generate, 16 "nonstructural" proteins, nsp1 to nsp16, involved in viral replication, and/or RNA processing. Among these, nsp10 plays a critical role in, minus-strand RNA synthesis in a related coronavirus, murine hepatitis, virus. Here, we report the crystal structure of SARS-CoV nsp10 at a, resolution of 1.8 A as determined by single-wavelength anomalous, dispersion using phases derived from hexatantalum dodecabromide. nsp10 is, a single domain protein consisting of a pair of antiparallel N-terminal, helices stacked against an irregular beta-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first, structural representative of this family of Zn finger proteins found so, far exclusively in coronaviruses. The first Zn finger coordinates a Zn2+, ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the "gag-knuckle fold group" of Zn2+-binding, domains and appears to maintain the structural integrity of the C-terminal, tail. A distinct clustering of basic residues on the protein surface, suggests a nucleic acid-binding function. Gel shift assays indicate that, in isolation, nsp10 binds single- and double-stranded RNA and DNA with, high-micromolar affinity and without obvious sequence specificity. It is, possible that nsp10 functions within a larger RNA-binding protein complex., However, its exact role within the replicase complex is still not clear.

About this Structure

2FYG is a Single protein structure of sequence from Human sars coronavirus with ZN and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs., Joseph JS, Saikatendu KS, Subramanian V, Neuman BW, Brooun A, Griffith M, Moy K, Yadav MK, Velasquez J, Buchmeier MJ, Stevens RC, Kuhn P, J Virol. 2006 Aug;80(16):7894-901. PMID:16873246

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