8UGC

FD15: Flat repeat helix-turn-helix-turn protein

8UGC の概要

• エントリーDOI: 10.2210/pdb8ugc/pdb
• 分子名称: FD15 (1 entity in total)
• 機能のキーワード: de novo 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: 77719.24

構造登録者

Davila-Hernandez, F.,Bera, A.K.,Kang, A.,Baker, D. (登録日: 2023-10-05, 公開日: 2023-12-27)

主引用文献

Davila-Hernandez, F.A.,Jin, B.,Pyles, H.,Zhang, S.,Wang, Z.,Huddy, T.F.,Bera, A.K.,Kang, A.,Chen, C.L.,De Yoreo, J.J.,Baker, D.
Directing polymorph specific calcium carbonate formation with de novo protein templates.
Nat Commun, 14:8191-8191, 2023

PubMed Abstract: Biomolecules modulate inorganic crystallization to generate hierarchically structured biominerals, but the atomic structure of the organic-inorganic interfaces that regulate mineralization remain largely unknown. We hypothesized that heterogeneous nucleation of calcium carbonate could be achieved by a structured flat molecular template that pre-organizes calcium ions on its surface. To test this hypothesis, we design helical repeat proteins (DHRs) displaying regularly spaced carboxylate arrays on their surfaces and find that both protein monomers and protein-Ca supramolecular assemblies directly nucleate nano-calcite with non-natural {110} or {202} faces while vaterite, which forms first in the absence of the proteins, is bypassed. These protein-stabilized nanocrystals then assemble by oriented attachment into calcite mesocrystals. We find further that nanocrystal size and polymorph can be tuned by varying the length and surface chemistry of the designed protein templates. Thus, bio-mineralization can be programmed using de novo protein design, providing a route to next-generation hybrid materials.

PubMed: 38097544
DOI: 10.1038/s41467-023-43608-1

実験手法

X-RAY DIFFRACTION (4 Å)