Premium
Proton‐decoupled 15 N and 31 P solid‐state NMR investigations of the Pf3 coat protein in oriented phospholipid bilayers
Author(s) -
Aisenbrey Christopher,
Harzer Ulrike,
BauerManz Gabriele,
Bär Gerda,
Chotimah Irma N. Husnal,
Bertani Philippe,
Sizun Christina,
Kuhn Andreas,
Bechinger Burkhard
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05114.x
Subject(s) - transmembrane protein , phospholipid , solid state nuclear magnetic resonance , crystallography , chemistry , nuclear magnetic resonance spectroscopy , coat protein , helix (gastropod) , membrane , lipid bilayer , membrane protein , transmembrane domain , biophysics , stereochemistry , biochemistry , nuclear magnetic resonance , biology , physics , rna , ecology , receptor , snail , gene
The coat proteins of filamentous phage are first synthesized as transmembrane proteins and then assembled onto the extruding viral particles. We investigated the transmembrane conformation of the Pseudomonas aeruginosa Pf3 phage coat protein using proton‐decoupled 15 N and 31 P solid‐state NMR spectroscopy. The protein was either biochemically purified and uniformly labelled with 15 N or synthesized chemically and labelled at specific sites. The proteins were then reconstituted into oriented phospholipid bilayers and the resulting samples analysed. The data suggest a model in which the protein adopts a tilted helix with an angle of ≈ 30° and an N‐terminal ‘swinging arm’ at the membrane surface.