1XAK

STRUCTURE OF THE SARS-CORONAVIRUS ORF7A ACCESSORY PROTEIN

Summary for 1XAK

• Entry DOI: 10.2210/pdb1xak/pdb
• Descriptor: SARS ORF7A ACCESSORY PROTEIN (2 entities in total)
• Functional Keywords: i-set ig domain, beta sandwich, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, viral protein
• Biological source: SARS coronavirus
• Cellular location: Virion: P59635
• Total number of polymer chains: 1
• Total formula weight: 9424.54

Authors

Nelson, C.A.,Lee, C.A.,Fremont, D.H.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2004-08-26, release date: 2004-10-05, Last modification date: 2024-10-30)

Primary citation

Nelson, C.A.,Pekosz, A.,Lee, C.A.,Diamond, M.S.,Fremont, D.H.
Structure and intracellular targeting of the SARS-coronavirus Orf7a accessory protein.
Structure, 13:75-85, 2005

PubMed Abstract: The open reading frame (ORF) 7a of the SARS-associated coronavirus (SARS-CoV) encodes a unique type I transmembrane protein of unknown function. We have determined the 1.8 A resolution crystal structure of the N-terminal ectodomain of orf7a, revealing a compact seven-stranded beta sandwich unexpectedly similar in fold and topology to members of the Ig superfamily. We also demonstrate that, in SARS-CoV- infected cells, the orf7a protein is expressed and retained intracellularly. Confocal microscopy studies using orf7a and orf7a/CD4 chimeras implicate the short cytoplasmic tail and transmembrane domain in trafficking of the protein within the endoplasmic reticulum and Golgi network. Taken together, our findings provide a structural and cellular framework in which to explore the role of orf7a in SARS-CoV pathogenesis.

PubMed: 15642263
DOI: 10.1016/j.str.2004.10.010

Experimental method

X-RAY DIFFRACTION (1.8 Å)