2CME

The crystal structure of SARS coronavirus ORF-9b protein

Summary for 2CME

• Entry DOI: 10.2210/pdb2cme/pdb
• Descriptor: HYPOTHETICAL PROTEIN 5, DECANE, ... (6 entities in total)
• Functional Keywords: alternative open reading frame, lipid-binding, virus assembly, hypothetical protein
• Biological source: HUMAN SARS CORONAVIRUS (SARS); More
• Cellular location: Host cytoplasmic vesicle membrane; Peripheral membrane protein: P59636 P59636 P59636 P59636
• Total number of polymer chains: 8
• Total formula weight: 68631.35

Authors

Meier, C.,Aricescu, A.R.,Assenberg, R.,Aplin, R.T.,Gilbert, R.J.C.,Grimes, J.M.,Stuart, D.I. (deposition date: 2006-05-06, release date: 2006-07-19, Last modification date: 2024-05-08)

Primary citation

Meier, C.,Aricescu, A.R.,Assenberg, R.,Aplin, R.T.,Gilbert, R.J.C.,Grimes, J.M.,Stuart, D.I.
The Crystal Structure of Orf-9B, a Lipid Binding Protein from the Sars Coronavirus.
Structure, 14:1157-, 2006

PubMed Abstract: 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.

PubMed: 16843897
DOI: 10.1016/J.STR.2006.05.012

Experimental method

X-RAY DIFFRACTION (2.8 Å)