1zy6

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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

Overview

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.

About this Structure

1ZY6 is a Single protein structure of sequence from [1] with NH2 as ligand. Full crystallographic information is available from OCA.

Reference

Membrane-bound dimer structure of a beta-hairpin antimicrobial peptide from rotational-echo double-resonance solid-state NMR., Mani R, Tang M, Wu X, Buffy JJ, Waring AJ, Sherman MA, Hong M, Biochemistry. 2006 Jul 11;45(27):8341-9. PMID:16819833

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