1DLZ

SOLUTION STRUCTURE OF THE CHANNEL-FORMER ZERVAMICIN IIB (PEPTAIBOL ANTIBIOTIC)

1DLZ の概要

• エントリーDOI: 10.2210/pdb1dlz/pdb
• 関連するPDBエントリー: 1AMT 1EE7 1GQ0 1IH9 1JOH 1M24 1OB4 1OB6 1OB7 1R9U
• NMR情報: BMRB: 4601
• 関連するBIRD辞書のPRD_ID: PRD_000159
• 分子名称: ZERVAMICIN IIB (1 entity in total)
• 機能のキーワード: zrevamicin, peptaibol, antibacterial, antifungal, antibiotic, bent helix
• 由来する生物種: EMERICELLOPSIS SALMOSYNNEMATA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1823.18

構造登録者

Balashova, T.A.,Shenkarev, Z.O.,Tagaev, A.A.,Ovchinnikova, T.V.,Raap, J.,Arseniev, A.S. (登録日: 1999-12-13, 公開日: 2000-02-03, 最終更新日: 2025-03-26)

主引用文献

Balashova, T.A.,Shenkarev, Z.O.,Tagaev, A.A.,Ovchinnikova, T.V.,Raap, J.,Arseniev, A.S.
NMR Structure of the Channel-Former Zervamicin Iib in Isotropic Solvents.
FEBS Lett., 466:333-, 2000

PubMed Abstract: Spatial structure of the membrane channel-forming hexadecapeptide, zervamicin IIB, was studied by NMR spectroscopy in mixed solvents of different polarity ranging from CDCl3/CD3OH (9:1, v/v) to CD3OH/H2O (1:1, v/v). The results show that in all solvents used the peptide has a very similar structure that is a bent amphiphilic helix with a mean backbone root mean square deviation (rmsd) value of ca. 0.3 A. Side chains of Trp1, Ile2, Gln3, Ile5 and Thr6 are mobile. The results are discussed in relation to the validity of the obtained structure to serve as a building block of zervamicin IIB ion channels.

PubMed: 10682854
DOI: 10.1016/S0014-5793(99)01707-X

実験手法

SOLUTION NMR