2CZP

Structural analysis of membrane-bound mastoparan-X by solid-state NMR

Summary for 2CZP

• Entry DOI: 10.2210/pdb2czp/pdb
• Related: 1A13 1D7N
• NMR Information: BMRB: 10001
• Descriptor: Mastoparan X (1 entity in total)
• Functional Keywords: mastoparan x, mp-x, membrane bound, mast cell degranulation, venom, amidation, toxin
• Biological source: Vespa simillima xanthoptera (Japanese yellow hornet)
• Cellular location: Secreted: P01515
• Total number of polymer chains: 1
• Total formula weight: 1557.99

Authors

Todokoro, Y.,Fujiwara, T.,Yumen, I.,Fukushima, K.,Kang, S.-W.,Park, J.-S.,Kohno, T.,Wakamatsu, K.,Akutsu, H. (deposition date: 2005-07-14, release date: 2006-07-04, Last modification date: 2024-11-13)

Primary citation

Todokoro, Y.,Yumen, I.,Fukushima, K.,Kang, S.-W.,Park, J.-S.,Kohno, T.,Wakamatsu, K.,Akutsu, H.,Fujiwara, T.
Structure of tightly membrane-bound mastoparan-x, a g-protein-activating Peptide, determined by solid-state NMR.
Biophys.J., 91:1368-1379, 2006

PubMed Abstract: The structure of mastoparan-X (MP-X), a G-protein activating peptide from wasp venom, in the state tightly bound to anionic phospholipid bilayers was determined by solid-state NMR spectroscopy. Carbon-13 and nitrogen-15 NMR signals of uniformly labeled MP-X were completely assigned by multidimensional intraresidue C-C, N-CalphaCbeta, and N-Calpha-C', and interresidue Calpha-CalphaCbeta, N-CalphaCbeta, and N-C'-Calpha correlation experiments. The backbone torsion angles were predicted from the chemical shifts of 13C', 13Calpha, 13Cbeta, and 15N signals with the aid of protein NMR database programs. In addition, two 13C-13C and three 13C-15N distances between backbone nuclei were precisely measured by rotational resonance and REDOR experiments, respectively. The backbone structure of MP-X was determined from the 26 dihedral angle restraints and five distances with an average root-mean-square deviation of 0.6 A. Peptide MP-X in the bilayer-bound state formed an amphiphilic alpha-helix for residues Trp3-Leu14 and adopted an extended conformation for Asn2. This membrane-bound conformation is discussed in relation to the peptide's activities to form pores in membranes and to activate G-proteins. This study demonstrates the power of multidimensional solid-state NMR of uniformly isotope-labeled molecules and distance measurements for determining the structures of peptides bound to lipid membranes.

PubMed: 16714348
DOI: 10.1529/biophysj.106.082735

Experimental method

SOLID-STATE NMR