2LIZ

NMR solution structure of C-terminal domain of SARS-CoV main protease in 2.5M urea

Summary for 2LIZ

• Entry DOI: 10.2210/pdb2liz/pdb
• NMR Information: BMRB: 17911
• Descriptor: 3C-like proteinase (1 entity in total)
• Functional Keywords: mpro-c sars-cov, hydrolase
• Biological source: SARS coronavirus (SARS-CoV)
• Cellular location: Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity): P0C6U8
• Total number of polymer chains: 1
• Total formula weight: 13282.98

Authors

Xia, B.,Kang, X. (deposition date: 2011-09-02, release date: 2012-09-05, Last modification date: 2024-11-20)

Primary citation

Kang, X.,Zhong, N.,Zou, P.,Zhang, S.,Jin, C.,Xia, B.
Foldon unfolding mediates the interconversion between M(pro)-C monomer and 3D domain-swapped dimer.
Proc.Natl.Acad.Sci.USA, 109:14900-14905, 2012

PubMed Abstract: The C-terminal domain (M(pro)-C) of SARS-CoV main protease adopts two different fold topologies, a monomer and a 3D domain-swapped dimer. Here, we report that M(pro)-C can reversibly interconvert between these two topological states under physiological conditions. Although the swapped α(1)-helix is fully buried inside the protein hydrophobic core, the interconversion of M(pro)-C is carried out without the hydrophobic core being exposed to solvent. The 3D domain swapping of M(pro)-C is activated by an order-to-disorder transition of its C-terminal α(5)-helix foldon. Unfolding of this foldon promotes self-association of M(pro)-C monomers and functions to mediate the 3D domain swapping, without which M(pro)-C can no longer form the domain-swapped dimer. Taken together, we propose that there exists a special dimeric intermediate enabling the protein core to unpack and the α(1)-helices to swap in a hydrophobic environment, which minimizes the energy cost of the 3D domain-swapping process.

PubMed: 22927388
DOI: 10.1073/pnas.1205241109

Experimental method

SOLUTION NMR