3WUI: Dimeric Horse Cytochrome C Formed By Refolding From Molten Globule State

Many proteins, including cytochrome c (cyt c), have been shown to form domain-swapped oligomers, but the factors governing the oligomerization process remain unrevealed. We obtained oligomers of cyt c by refolding cyt c from its acid molten globule state to neutral pH state under high protein and ion concentrations. The amount of oligomeric cyt c obtained depended on the nature of the anion (chaotropic or kosmotropic) in the solution: ClO4- (oligomers, 11% +/- 2% (heme unit)), SCN- (10% +/- 2%), I- (6% +/- 2%), NO3- (3% +/- 1%), Br- (2% +/- 1%), Cl- (2% +/- 1%), and SO42- (3% +/- 1%) for refolding of 2 mM cyt c (anion concentration 125 mM). Dimeric cyt c obtained by refolding from the molten globule state exhibited a domain-swapped structure, in which the C-terminal alpha-helices were exchanged between protomers. According to small-angle X-ray scattering measurements, approximately 25% of the cyt c molecules were dimerized in the molten globule state containing 125 mM ClO4-. These results indicate that a certain amount of molten globule state oligomers of cyt c convert to domain-swapped oligomers during refolding and that the intermolecular interactions necessary for domain swapping are present in the molten globule state.
PDB ID: 3WUIDownload
MMDB ID: 121438
PDB Deposition Date: 2014/4/25
Updated in MMDB: 2014/07
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3WUI: dimeric; determined by author and by software (PISA)
Molecular Components in 3WUI
Label Count Molecule
Proteins (2 molecules)
Cytochrome C(Gene symbol: CYCS)
Molecule annotation
Chemicals (9 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB