5EON

Crystal structure of a de novo antiparallel coiled-coil hexamer - ACC-Hex

5EON の概要

• エントリーDOI: 10.2210/pdb5eon/pdb
• 分子名称: ACC-Hex (2 entities in total)
• 機能のキーワード: hexamer, coiled-coil, antiparallel, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 10055.99

構造登録者

Spencer, R.K.,Hochbaum, A.I. (登録日: 2015-11-10, 公開日: 2016-05-25, 最終更新日: 2024-11-20)

主引用文献

Spencer, R.K.,Hochbaum, A.I.
X-ray Crystallographic Structure and Solution Behavior of an Antiparallel Coiled-Coil Hexamer Formed by de Novo Peptides.
Biochemistry, 55:3214-3223, 2016

PubMed Abstract: The self-assembly of peptides and proteins into higher-ordered structures is encoded in the amino acid sequence of each peptide or protein. Understanding the relationship among the amino acid sequence, the assembly dynamics, and the structure of well-defined peptide oligomers expands the synthetic toolbox for these structures. Here, we present the X-ray crystallographic structure and solution behavior of de novo peptides that form antiparallel coiled-coil hexamers (ACC-Hex) by an interaction motif neither found in nature nor predicted by existing peptide design software. The 1.70 Å X-ray crystallographic structure of peptide 1a shows six α-helices associating in an antiparallel arrangement around a central axis comprising hydrophobic and aromatic residues. Size-exclusion chromatography studies suggest that peptides 1 form stable oligomers in solution, and circular dichroism experiments show that peptides 1 are stable to relatively high temperatures. Small-angle X-ray scattering studies of the solution behavior of peptide 1a indicate an equilibrium of dimers, hexamers, and larger aggregates in solution. The structures presented here represent a new motif of biomolecular self-assembly not previously observed for de novo peptides and suggest supramolecular design principles for material scaffolds based on coiled-coil motifs containing aromatic residues.

PubMed: 27192036
DOI: 10.1021/acs.biochem.6b00201

実験手法

X-RAY DIFFRACTION (1.696 Å)