Domain-swapped cytochrome cb₅₆₂ dimer and its nanocage encapsulating a Zn-SO₄ cluster in the internal cavity.

ABSTRACT: Protein nanostructures have been gaining in interest, along with developments in new methods for construction of novel nanostructures. We have previously shown that c-type cytochromes and myoglobin form oligomers by domain swapping. Herein, we show that a four-helix bundle protein cyt cb₅₆₂, with the cyt b₅₆₂ heme attached to the protein moiety by two Cys residues insertion, forms a domain-swapped dimer. Dimeric cyt cb₅₆₂ did not dissociate to monomers at 4 °C, whereas dimeric cyt b₅₆₂ dissociated under the same conditions, showing that heme attachment to the protein moiety stabilizes the domain-swapped structure. According to X-ray crystallographic analysis of dimeric cyt cb₅₆₂, the two helice

SUBMITTER: Miyamoto T 

PROVIDER: S-EPMC5519777 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature