2ORL

Solution structure of the cytochrome c- para-aminophenol adduct

2ORL の概要

• エントリーDOI: 10.2210/pdb2orl/pdb
• 関連するPDBエントリー: 2HV4
• 分子名称: Cytochrome c iso-1, HEME C, 4-AMINOPHENOL (3 entities in total)
• 機能のキーワード: protein-ligand adduct, electron transport
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Mitochondrion intermembrane space: P00044
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12799.43

構造登録者

Assfalg, M.,Bertini, I.,Del Conte, R.,Giachetti, A.,Turano, P. (登録日: 2007-02-03, 公開日: 2007-04-24, 最終更新日: 2024-10-30)

主引用文献

Assfalg, M.,Bertini, I.,Del Conte, R.,Giachetti, A.,Turano, P.
Cytochrome c and organic molecules: solution structure of the p-aminophenol adduct.
Biochemistry, 46:6232-6238, 2007

PubMed Abstract: Protein-protein interactions are driven by specific properties of the molecular surfaces. Cytochrome c, a small electron transfer protein, is involved in a number of biologically relevant interactions with macromolecular partners. Small molecules may interfere with such interactions by binding to the surface of cytochrome c. Here we investigated the possibility of weak intermolecular interactions between reduced cytochrome c and a library of 325 small molecules, using WaterLOGSY NMR spectroscopy. Specific binding was found for p-aminophenol. The solution structure of the p-aminophenol-cytochrome c adduct was determined using a combination of in silico tools and NMR-based restraints. The ligand interacts in a specific binding site on the protein surface through a combination of stacking and H-bond interactions. Small but meaningful rearrangements of the solvent-exposed side chains are observed upon ligand binding and contribute to the stabilization of the complex.

PubMed: 17488096
DOI: 10.1021/bi7002857

実験手法

SOLUTION NMR