Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein
Publication date
2005
Authors
Duquerroy, Stéphane
Vigouroux, Armelle
Rottier, P.J.M.
Rey, Félix A
Bosch, Berend-Jan
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Document Type
Article
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Abstract
The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix.
Keywords
Amino Acid Sequence, Asparagine, Glutamine, Ions, Membrane Fusion, Membrane Glycoproteins, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, SARS Virus, Salts, Spike Glycoprotein, Coronavirus, Static Electricity, Thermodynamics, Viral Envelope Proteins, Coronacrisis-Taverne
Citation
Duquerroy, S, Vigouroux, A, Rottier, P J M, Rey, F A & Bosch, B J 2005, 'Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein', Virology, vol. 335, no. 2, pp. 276-85. https://doi.org/10.1016/j.virol.2005.02.022