3NWV
Human cytochrome c G41S
Summary for 3NWV
| Entry DOI | 10.2210/pdb3nwv/pdb |
| Descriptor | Cytochrome c, HEME C (3 entities in total) |
| Functional Keywords | cytochrome, electron transport, apaf-1, heme, mitochondia, apoptosis |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 49156.44 |
| Authors | Fagerlund, R.D.,Wilbanks, S.M. (deposition date: 2010-07-11, release date: 2011-03-09, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 21192676DOI: 10.1021/ja106328k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
