9OXP

Beta-barrel forming peptide macrocycle

Summary for 9OXP

• Entry DOI: 10.2210/pdb9oxp/pdb
• Descriptor: MC4HH3AH10D (ORN)WFHSH(ORN)FI(MHS)(SAR)H peptide macrocycle, ACETATE ION (3 entities in total)
• Functional Keywords: macrocycle, beta-barrel, beta-sheet, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 2
• Total formula weight: 3186.61

Authors

Dang, V.T.,Nguyen, A. (deposition date: 2025-06-04, release date: 2026-01-07, Last modification date: 2026-02-11)

Primary citation

Dang, V.T.,Martynowycz, M.W.,McElheny, D.,Nguyen, A.I.
beta-barrels from short macrocyclic peptides.
Chem.Commun.(Camb.), 62:2304-2308, 2026

PubMed Abstract: β-Barrels are ubiquitous motifs in protein structures, but the fundamental rules underlying their formation are unclear, and their design remains highly challenging. Small peptides that form barrels are especially scarce. Here, we report barrels with the shortest staves (6 residues, ∼60% of previous record) and smallest shear number ( = 4) so far, formed from 12-residue macrocyclic peptides. The miniature barrel has anomalous structural features, demonstrated by solution phase and crystallographic characterization; there is a pronounced and essential backbone kink imparted by an achiral residue, -methylglycine, as well as four structural water molecules stitching the seams of the barrel. These results provide insights into how extremely short sequences could form barrel assemblies.

PubMed: 41489626
DOI: 10.1039/d5cc06640a

Experimental method

X-RAY DIFFRACTION (1.2 Å)