5ET3

Crystal Structure of De novo Designed Fullerene organizing peptide

Summary for 5ET3

• Entry DOI: 10.2210/pdb5et3/pdb
• Descriptor: Fullerene Organizing Protein (C60Sol-COP-3), (C_{60}-I_{h})[5,6]fullerene (3 entities in total)
• Functional Keywords: de novo protein, fullerene, complex, helical assembly
• Biological source: synthetic construct
• Total number of polymer chains: 2
• Total formula weight: 7097.77

Authors

Kim, K.-H.,Kim, Y.H.,Acharya, R.,Kim, N.H.,Paul, J.,Grigoryan, G.,DeGrado, W.F. (deposition date: 2015-11-17, release date: 2016-05-04, Last modification date: 2023-11-08)

Primary citation

Kim, K.-H.,Ko, D.-K.,Kim, Y.-T.,Kim, N.H.,Paul, J.,Zhang, S.-Q.,Murray, C.B.,Acharya, R.,DeGrado, W.F.,Kim, Y.H.,Grigoryan, G.
Protein-directed self-assembly of a fullerene crystal.
Nat Commun, 7:11429-11429, 2016

PubMed Abstract: Learning to engineer self-assembly would enable the precise organization of molecules by design to create matter with tailored properties. Here we demonstrate that proteins can direct the self-assembly of buckminsterfullerene (C60) into ordered superstructures. A previously engineered tetrameric helical bundle binds C60 in solution, rendering it water soluble. Two tetramers associate with one C60, promoting further organization revealed in a 1.67-Å crystal structure. Fullerene groups occupy periodic lattice sites, sandwiched between two Tyr residues from adjacent tetramers. Strikingly, the assembly exhibits high charge conductance, whereas both the protein-alone crystal and amorphous C60 are electrically insulating. The affinity of C60 for its crystal-binding site is estimated to be in the nanomolar range, with lattices of known protein crystals geometrically compatible with incorporating the motif. Taken together, these findings suggest a new means of organizing fullerene molecules into a rich variety of lattices to generate new properties by design.

PubMed: 27113637
DOI: 10.1038/ncomms11429

Experimental method

X-RAY DIFFRACTION (1.671 Å)