2cme

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2cme, resolution 2.8Å

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THE CRYSTAL STRUCTURE OF SARS CORONAVIRUS ORF-9B PROTEIN

Overview

To achieve the greatest output from their limited genomes, viruses, frequently make use of alternative open reading frames, in which, translation is initiated from a start codon within an existing gene and, being out of frame, gives rise to a distinct protein product. These, alternative protein products are, as yet, poorly characterized, structurally. Here we report the crystal structure of ORF-9b, an, alternative open reading frame within the nucleocapsid (N) gene from the, SARS coronavirus. The protein has a novel fold, a dimeric tent-like beta, structure with an amphipathic surface, and a central hydrophobic cavity, that binds lipid molecules. This cavity is likely to be involved in, membrane attachment and, in mammalian cells, ORF-9b associates with, intracellular vesicles, consistent with a role in the assembly of the, virion. Analysis of ORF-9b and other overlapping genes suggests that they, provide snapshots of the early evolution of novel protein folds.

About this Structure

2CME is a Single protein structure of sequence from Human sars coronavirus with D10 as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of ORF-9b, a lipid binding protein from the SARS coronavirus., Meier C, Aricescu AR, Assenberg R, Aplin RT, Gilbert RJ, Grimes JM, Stuart DI, Structure. 2006 Jul;14(7):1157-65. PMID:16843897

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