5HKN

Crystal structure de novo designed fullerene organizing protein complex with fullerene

5HKN の概要

• エントリーDOI: 10.2210/pdb5hkn/pdb
• 関連するPDBエントリー: 5HKR
• 分子名称: fullerene organizing protein, (C_{60}-I_{h})[5,6]fullerene (3 entities in total)
• 機能のキーワード: fullerene protein complex, de novo protein design, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7097.77

構造登録者

Paul, J.,Acharya, R.,Kim, K.-H.,Kim, Y.H.,Kim, N.H.,Grigoryan, G.,DeGardo, W.F. (登録日: 2016-01-14, 公開日: 2016-05-04, 最終更新日: 2023-11-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.761 Å)