2cme

From PDBWiki

Authors	Meier, C. Aricescu, A.R. Assenberg, R. Aplin, R.T. Gilbert, R.J. Grimes, J.M. Stuart, D.I.
Citation	The crystal structure of ORF-9b, a lipid binding protein from the SARS coronavirus. PubMed
Release date	2006-07-19
Exp. Method	X-RAY DIFFRACTION
Resolution	2.8 Å
Classification	HYPOTHETICAL PROTEIN

Sequence

Chain(s) A (78 residues): Blast

VPPALHLVDPQIQLTITADPKVYPIILRLGSNLSLSMARRNLDSLEARAFQSTPIVVQMTKLATTEELPDEFVVVTAK

Chain(s) B (79 residues): Blast

VPPALHLVDPQIQLTITRADPKVYPIILRLGSNLSLSMARRNLDSLEARAFQSTPIVVQMTKLATTEELPDEFVVVTAK

Chain(s) C D F H (76 residues): Blast

PPALHLVDPQIQLTITDPKVYPIILRLGSNLSLSMARRNLDSLEARAFQSTPIVVQMTKLATTEELPDEFVVVTAK

Chain(s) E G (77 residues): Blast

VPPALHLVDPQIQLTITDPKVYPIILRLGSNLSLSMARRNLDSLEARAFQSTPIVVQMTKLATTEELPDEFVVVTAK

User comments

ORF9b is a small protein encoded by the genome of the SARS virus. When the virus was first discovered and characterised, the function of the protein was unknown.

The structure of the protein, reported here, reveals that ORF-9b is a lipid-binding protein which can associate with cellular membranes, suggesting that the protein may play a role in the assembly of the SARS virus particle (the virion consists of a nucleoprotein core surrounded by a lipid envelope). Subsequence functional studies have shown that ORF 9b interacts with many other SARS proteins, consistent with its putative role in assembly [von Brunn et al. (2007) PLoS ONE 2(5):e459]

The structure of ORF-9b represents a novel fold -- a dimeric tent-like beta structure with an amphipathic surface, and a central hydrophobic cavity that binds lipid molecules.

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