1ZY6

Membrane-bound dimer structure of Protegrin-1 (PG-1), a beta-Hairpin Antimicrobial Peptide in Lipid Bilayers from Rotational-Echo Double-Resonance Solid-State NMR

Summary for 1ZY6

• Entry DOI: 10.2210/pdb1zy6/pdb
• Related: 1PG1
• Descriptor: Protegrin 1 (1 entity in total)
• Functional Keywords: beta-hairpin, solid state nmr, antibiotic
• Cellular location: Secreted: P32194
• Total number of polymer chains: 2
• Total formula weight: 4329.36

Authors

Wu, X.,Mani, R.,Tang, M.,Buffy, J.J.,Waring, A.J.,Sherman, M.A.,Hong, M. (deposition date: 2005-06-09, release date: 2006-06-13, Last modification date: 2022-03-02)

Primary citation

Mani, R.,Tang, M.,Wu, X.,Buffy, J.J.,Waring, A.J.,Sherman, M.A.,Hong, M.
Membrane-Bound Dimer Structure of a beta-Hairpin Antimicrobial Peptide from Rotational-Echo Double-Resonance Solid-State NMR.
Biochemistry, 45:8341-8349, 2006

PubMed Abstract: The intermolecular packing of a beta-hairpin antimicrobial peptide, PG-1, in lipid bilayers is determined using solid-state NMR distance measurements. Previous spin counting experiments showed that PG-1 associates as dimers in POPC bilayers; however, the detailed dimer structure was unknown. We have now measured several intermolecular 13C-19F, 1H-13C, and 15N-13C distances in site-specifically labeled PG-1 to constrain the structure of the intermolecular interface. The distances are measured using the rotational-echo double-resonance (REDOR) technique under magic-angle spinning. The results indicate that two PG-1 molecules align in a parallel fashion with the C-terminal strand of the hairpin forming the dimer interface. Six hydrogen bonds stabilize this interface, and the Phe12 side chain adopts the g- conformation in the membrane as in solution. The parallel packing of the peptide in the lipid bilayer differs from the antiparallel dimer found in DPC micelles and may be stabilized by its strong amphipathic character, which should facilitate its insertion into the amphipathic lipid bilayer. This study demonstrates the utility of the REDOR NMR technique for the elucidation of the oligomeric structure of membrane proteins.

PubMed: 16819833
DOI: 10.1021/bi060305b

Experimental method

SOLID-STATE NMR