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
Complex formation between cationic cytochrome c and the water-soluble, poly-anionic p-phosphonatocalix[6]arene (pclx6 ) was investigated. A crystal structure (at 1.8 A resolution) revealed a remarkable dimeric disc of pclx6 that acts like glue to mediate a symmetric (C2 ) protein dimer. The calixarene disc has a diameter of about 1.5 nm and masks about 360 A2 of protein surface. The key protein-calixarene contacts occur via two linchpin lysines, with additional contacts provided by a small hydrophobic patch. The protein-calixarene supramolecular assemblies were observed in solution by size-exclusion chromatography with multi-angle light scattering and NMR spectroscopy. Using isothermal titration calorimetry and NMR data, an apparent Kd in the low micromolar range was determined for the charge-rich protein-calixarene complex. In contrast to p-sulfonatocalix[4]arene, the larger pclx6 has a single, well-defined binding site that mediates the assembly of cytochrome c in solution.
Protein Dimerization on a Phosphonated Calix[6]arene Disc.,Rennie ML, Doolan AM, Raston CL, Crowley PB Angew Chem Int Ed Engl. 2017 May 8;56(20):5517-5521. doi: 10.1002/anie.201701500., Epub 2017 Apr 13. PMID:28407337[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rennie ML, Doolan AM, Raston CL, Crowley PB. Protein Dimerization on a Phosphonated Calix[6]arene Disc. Angew Chem Int Ed Engl. 2017 May 8;56(20):5517-5521. doi: 10.1002/anie.201701500., Epub 2017 Apr 13. PMID:28407337 doi:http://dx.doi.org/10.1002/anie.201701500
