Structural highlights
Function
CYC1_YEAST Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
Publication Abstract from PubMed
Co-crystallization of a 2 kDa tether-free sulfonated foldamer and the 13 kDa lysine-rich cytochrome c yielded a remarkable biohybrid assembly with chiral resolution of the foldamer helix handedness. In the crystal a approximately 5 nm foldamer stack was surrounded by eight molecules of protein. NMR and CD experiments suggest interesting differences in the solution state recognition processes.
Crystal structure of a protein-aromatic foldamer composite: macromolecular chiral resolution.,Alex JM, Corvaglia V, Hu X, Engilberge S, Huc I, Crowley PB Chem Commun (Camb). 2019 Sep 21;55(74):11087-11090. doi: 10.1039/c9cc05330a. Epub , 2019 Aug 28. PMID:31460523[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alex JM, Corvaglia V, Hu X, Engilberge S, Huc I, Crowley PB. Crystal structure of a protein-aromatic foldamer composite: macromolecular chiral resolution. Chem Commun (Camb). 2019 Sep 21;55(74):11087-11090. PMID:31460523 doi:10.1039/c9cc05330a
