7QDI

Structure of octameric left-handed 310-helix bundle: D-310HD

7QDI の概要

• エントリーDOI: 10.2210/pdb7qdi/pdb
• 分子名称: D-310HD, TRIETHYLENE GLYCOL, 1,2-ETHANEDIOL, ... (10 entities in total)
• 機能のキーワード: octamer, 310-helix, ll core, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 30058.57

構造登録者

Kumar, P.,Paterson, N.G.,Woolfson, D.N. (登録日: 2021-11-27, 公開日: 2022-04-27, 最終更新日: 2022-07-27)

主引用文献

Kumar, P.,Paterson, N.G.,Clayden, J.,Woolfson, D.N.
De novo design of discrete, stable 3 10 -helix peptide assemblies.
Nature, 607:387-392, 2022

PubMed Abstract: The α-helix is pre-eminent in structural biology and widely exploited in protein folding, design and engineering. Although other helical peptide conformations do exist near to the α-helical region of conformational space-namely, 3-helices and π-helices-these occur much less frequently in protein structures. Less favourable internal energies and reduced tendencies to pack into higher-order structures mean that 3-helices rarely exceed six residues in length in natural proteins, and that they tend not to form normal supersecondary, tertiary or quaternary interactions. Here we show that despite their absence in nature, synthetic peptide assemblies can be built from 3-helices. We report the rational design, solution-phase characterization and an X-ray crystal structure for water-soluble bundles of 3-helices with consolidated hydrophobic cores. The design uses six-residue repeats informed by analysing 3-helical conformations in known protein structures, and incorporates α-aminoisobutyric acid residues. Design iterations reveal a tipping point between α-helical and 3-helical folding, and identify features required for stabilizing assemblies of 3-helices. This work provides principles and rules to open opportunities for designing into this hitherto unexplored region of protein-structure space.

PubMed: 35732733
DOI: 10.1038/s41586-022-04868-x

実験手法

X-RAY DIFFRACTION (2.34 Å)