Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 37, Pages 14900-14905Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1205241109
Keywords
NMR; protein folding
Categories
Funding
- 973 Program of China [2012CB910700, 2011IM030300, 2003CB514104]
- NSFC of China [31170682]
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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 alpha(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 alpha(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 alpha(1)-helices to swap in a hydrophobic environment, which minimizes the energy cost of the 3D domain-swapping process.
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