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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 cb  562 , with the cyt b  562 heme attached to the protein moiety by two Cys residues insertion, forms a domain-swapped dimer. Dimeric cyt cb  562 did not dissociate to monomers at 4 °C, whereas dimeric cyt b  562 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 cb  562 , the two helices in the N-terminal region of one protomer interacted with the other two helices in the C-terminal region of the other protomer, where Lys51-Asp54 served as a hinge loop. The heme coordination structure of the dimer was similar to that of the monomer. In the crystal, three domain-swapped cyt cb  562 dimers formed a unique cage structure with a Zn-SO 4 cluster inside the cavity. The Zn-SO 4 cluster consisted of fifteen Zn 2+ and seven SO 4  2- ions, whereas six additional Zn 2+ ions were detected inside the cavity. The cage structure was stabilized by coordination of the amino acid side chains of the dimers to the Zn 2+ ions and connection of two four-helix bundle units through the conformation-adjustable hinge loop. These results show that domain swapping can be applied in the construction of unique protein nanostructures.

Domain-swapped cytochrome cb562dimer and its nanocage encapsulating a Zn–SO4cluster in the internal cavity

Domain-swapped cytochrome cb₅₆₂dimer and its nanocage encapsulating a Zn–SO₄cluster in the internal cavity