7OWX

Structure of coiled-coil tetramer from SARS-CoV-2 spike stalk region

Summary for 7OWX

• Entry DOI: 10.2210/pdb7owx/pdb
• Descriptor: Spike protein S2, 1,2-ETHANEDIOL, ZINC ION, ... (4 entities in total)
• Functional Keywords: spike, sars-cov-2, coiled-coil, tetramer, virus, coronavirus, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• Total number of polymer chains: 4
• Total formula weight: 13191.39

Authors

Zivic, Z.,Hadzi, S. (deposition date: 2021-06-21, release date: 2022-03-16, Last modification date: 2024-06-19)

Primary citation

Zivic, Z.,Strmsek, Z.,Novinec, M.,Lah, J.,Hadzi, S.
Structural polymorphism of coiled-coils from the stalk domain of SARS-CoV-2 spike protein.
Faseb J., 36:e22199-e22199, 2022

PubMed Abstract: Spike trimer plays a key role in SARS-CoV-2 infection and vaccine development. It consists of a globular head and a flexible stalk domain that anchors the protein into the viral membrane. While the head domain has been extensively studied, the properties of the adjoining stalk are poorly understood. Here, we characterize the coiled-coil formation and thermodynamic stability of the stalk domain and its segments. We find that the N-terminal segment of the stalk does not form coiled-coils and remains disordered in solution. The C-terminal stalk segment forms a trimeric coiled-coil in solution, which becomes significantly stabilized in the context of the full-length stalk. Its crystal structure reveals a novel antiparallel tetramer coiled-coil with an unusual combination of a-d and e-a-d hydrophobic core packing. Structural analysis shows that a subset of hydrophobic residues stabilizes different coiled-coil structures: trimer, tetramer, and heterohexamer, underscoring a highly polymorphic nature of the SARS-CoV-2 stalk sequence.

PubMed: 35157347
DOI: 10.1096/fj.202101670R

Experimental method

X-RAY DIFFRACTION (1.929 Å)