2CZP

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

2CZP の概要

• エントリーDOI: 10.2210/pdb2czp/pdb
• 関連するPDBエントリー: 1A13 1D7N
• NMR情報: BMRB: 10001
• 分子名称: Mastoparan X (1 entity in total)
• 機能のキーワード: mastoparan x, mp-x, membrane bound, mast cell degranulation, venom, amidation, toxin
• 由来する生物種: Vespa simillima xanthoptera (Japanese yellow hornet)
• 細胞内の位置: Secreted: P01515
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1557.99

構造登録者

Todokoro, Y.,Fujiwara, T.,Yumen, I.,Fukushima, K.,Kang, S.-W.,Park, J.-S.,Kohno, T.,Wakamatsu, K.,Akutsu, H. (登録日: 2005-07-14, 公開日: 2006-07-04, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

SOLID-STATE NMR