1AY3

Nodularin from Nodularia spumigena

1AY3 の概要

• エントリーDOI: 10.2210/pdb1ay3/pdb
• 分子名称: PEPTIDIC TOXIN NODULARIN (1 entity in total)
• 機能のキーワード: hepatotoxin, inhibitor of ser/thr-specific protein phosphatases, toxin
• 由来する生物種: Nodularia spumigena
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 843.99

構造登録者

Annila, A.J. (登録日: 1997-11-14, 公開日: 1999-08-16, 最終更新日: 2023-11-15)

主引用文献

Annila, A.,Lehtimaki, J.,Mattila, K.,Eriksson, J.E.,Sivonen, K.,Rantala, T.T.,Drakenberg, T.
Solution structure of nodularin. An inhibitor of serine/threonine-specific protein phosphatases.
J.Biol.Chem., 271:16695-16702, 1996

PubMed Abstract: The three-dimensional solution structure of nodularin was studied by NMR and molecular dynamics simulations. The conformation in water was determined from the distance and dihedral data by distance geometry and refined by iterative relaxation matrix analysis. The cyclic backbone adopts a well defined conformation but the remote parts of the side chains of arginine as well as the amino acid derivative Adda have a large spatial dispersion. For the unusual amino acids the partial charges were calculated and nodularin was subjected to molecular dynamic simulations in water. A good agreement was found between experimental and computational data with hydrogen bonds, solvent accessibility, molecular motion, and conformational exchange. The three-dimensional structure resembles very closely that of microcystin-LR in the chemically equivalent segment. Therefore, it is expected that the binding of both microcystins and nodularins to serine/threonine-specific protein phosphatases is similar on an atomic level.

PubMed: 8663277
DOI: 10.1074/jbc.271.28.16695

実験手法

SOLUTION NMR