6GD6
Cytochrome c in complex with Sulfonato-calix[8]arene, H3 form with ammonium sulfate
Summary for 6GD6
| Entry DOI | 10.2210/pdb6gd6/pdb |
| Related | 6GD7 6GD8 6GD9 6GDA |
| Descriptor | Cytochrome c iso-1, HEME C, sulfonato-calix[8]arene, ... (5 entities in total) |
| Functional Keywords | calixarene, scaffold, supramolecular, assembly, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) |
| Total number of polymer chains | 1 |
| Total formula weight | 14630.07 |
| Authors | Rennie, M.L.,Fox, G.C.,Crowley, P.B. (deposition date: 2018-04-23, release date: 2018-08-29, Last modification date: 2024-10-16) |
| Primary citation | Rennie, M.L.,Fox, G.C.,Perez, J.,Crowley, P.B. Auto-regulated Protein Assembly on a Supramolecular Scaffold. Angew. Chem. Int. Ed. Engl., 57:13764-13769, 2018 Cited by PubMed Abstract: Controlled protein assembly provides a means to regulate function. Supramolecular building blocks, including rigid macrocycles, are versatile triggers of protein assembly. Now it is shown that sulfonato-calix[8]arene (sclx ) mediates the formation of cytochrome c tetramers in solution. This tetramer spontaneously disassembles at ≥2 equivalents of sclx , providing a remarkable example of auto-regulation. Using X-ray crystallography the sclx binding sites on cytochrome c were characterized. Crystal structures at different protein-ligand ratios reveal varying degrees (up to 35 %) of protein surface coverage by the flexible calixarene and suggest a mechanism for oligomer disassembly. The solution structure of the oligomer was characterized by small-angle X-ray scattering. Overall, the data indicate calixarene-controlled protein assembly and disassembly without the requirement for a competitive inhibitor, and point to protein encapsulation by a flexible macrocycle. PubMed: 30109907DOI: 10.1002/anie.201807490 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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