3NWV

Human cytochrome c G41S

3NWV の概要

• エントリーDOI: 10.2210/pdb3nwv/pdb
• 分子名称: Cytochrome c, HEME C (3 entities in total)
• 機能のキーワード: cytochrome, electron transport, apaf-1, heme, mitochondia, apoptosis
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49156.44

構造登録者

Fagerlund, R.D.,Wilbanks, S.M. (登録日: 2010-07-11, 公開日: 2011-03-09, 最終更新日: 2024-10-30)

主引用文献

Liptak, M.D.,Fagerlund, R.D.,Ledgerwood, E.C.,Wilbanks, S.M.,Bren, K.L.
The Proapoptotic G41S Mutation to Human Cytochrome c Alters the Heme Electronic Structure and Increases the Electron Self-Exchange Rate.
J.Am.Chem.Soc., 133:1153-1155, 2011

PubMed Abstract: The naturally occurring G41S mutation to human (Hs) cytochrome (cyt) c enhances apoptotic activity based upon previous in vitro and in vivo studies, but the molecular mechanism underlying this enhancement remains unknown. Here, X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and density functional theory (DFT) calculations have been used to identify the structural and electronic differences between wild-type (WT) and G41S Hs cyt c. S41 is part of the hydrogen bonding network for propionate 7 of heme pyrrole ring A in the X-ray structure of G41S Hs cyt c and, compared to WT, G41S Hs cyt c has increased spin density on pyrrole ring C and a faster electron self-exchange rate. DFT calculations illustrate an electronic mechanism where structural changes near ring A can result in electronic changes at ring C. Since ring C is part of the solvent-exposed protein surface, we propose that this heme electronic structure change may ultimately be responsible for the enhanced proapoptotic activity of G41S Hs cyt c.

PubMed: 21192676
DOI: 10.1021/ja106328k

実験手法

X-RAY DIFFRACTION (1.9 Å)