1ZV8

A structure-based mechanism of SARS virus membrane fusion

Summary for 1ZV8

• Entry DOI: 10.2210/pdb1zv8/pdb
• Related: 1ZV7 1ZVA 1ZVB
• Descriptor: E2 glycoprotein, SODIUM ION, CACODYLATE ION, ... (7 entities in total)
• Functional Keywords: sars coronavirus, membrane fusion, s2, virus entry, coiled coils, conformational change, viral protein
• Biological source: SARS coronavirus; More
• Cellular location: Virion membrane; Single-pass type I membrane protein: P59594 P59594
• Total number of polymer chains: 12
• Total formula weight: 57131.89

Authors

Deng, Y.,Liu, J.,Zheng, Q.,Yong, W.,Dai, J.,Lu, M. (deposition date: 2005-06-01, release date: 2006-05-16, Last modification date: 2024-02-14)

Primary citation

Deng, Y.,Liu, J.,Zheng, Q.,Yong, W.,Lu, M.
Structures and Polymorphic Interactions of Two Heptad-Repeat Regions of the SARS Virus S2 Protein.
Structure, 14:889-899, 2006

PubMed Abstract: Entry of SARS coronavirus into its target cell requires large-scale structural transitions in the viral spike (S) glycoprotein in order to induce fusion of the virus and cell membranes. Here we describe the identification and crystal structures of four distinct alpha-helical domains derived from the highly conserved heptad-repeat (HR) regions of the S2 fusion subunit. The four domains are an antiparallel four-stranded coiled coil, a parallel trimeric coiled coil, a four-helix bundle, and a six-helix bundle that is likely the final fusogenic form of the protein. When considered together, the structural and thermodynamic features of the four domains suggest a possible mechanism whereby the HR regions, initially sequestered in the native S glycoprotein spike, are released and refold sequentially to promote membrane fusion. Our results provide a structural framework for understanding the control of membrane fusion and should guide efforts to intervene in the SARS coronavirus entry process.

PubMed: 16698550
DOI: 10.1016/j.str.2006.03.007

Experimental method

X-RAY DIFFRACTION (1.94 Å)