3F87: An alpha/beta-Peptide Helix Bundle with a Pure beta-Amino Acid Core and a Distinctive Quarternary Structure: GCN4pLI derivative with beta residues at a and d heptad positions - higher symmetry crystal

Helix bundles are among the most widely studied tertiary and quaternary structural motifs in proteins. Here we present the crystal structure of an alpha/beta-peptide foldamer that adopts a tetrameric helix-bundle quaternary structure with a hydrophobic core composed solely of beta-amino acids. The structure displays features that are unprecedented among all known helix bundles composed of either alpha-peptides or peptidic foldamers. The tetramer is characterized by an asymmetry of interaction between neighboring helices, and the side-chain packing within the hydrophobic core differs fundamentally from the knobs-into-holes arrangement typical of most helix bundles.
PDB ID: 3F87Download
MMDB ID: 75444
PDB Deposition Date: 2008/11/11
Updated in MMDB: 2009/08
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 3F87: tetrameric; determined by author
Molecular Components in 3F87
Label Count Molecule
Proteins (4 molecules)
Molecule annotation
Chemicals (10 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB