5EOJ

Crystal structure of an antiparallel hexamer coiled-coil - ACC-Hex-PheI

Summary for 5EOJ

• Entry DOI: 10.2210/pdb5eoj/pdb
• Descriptor: ACC-Hex-PheI (2 entities in total)
• Functional Keywords: coiled-coil, hexamer, heptad repeat, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 3
• Total formula weight: 10316.57

Authors

Spencer, R.K.,Hochbaum, A.I. (deposition date: 2015-11-10, release date: 2016-05-25, Last modification date: 2022-12-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.115 Å)