5LYC
Cytochrome c in complex with phosphonato-calix[6]arene
Summary for 5LYC
| Entry DOI | 10.2210/pdb5lyc/pdb |
| Descriptor | Cytochrome c iso-1, HEME C, phosphonato-calix[6]arene, ... (5 entities in total) |
| Functional Keywords | calixarene, dimer, surface-binding, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 28034.08 |
| Authors | Rennie, M.L.,Crowley, P.B. (deposition date: 2016-09-27, release date: 2017-05-10, Last modification date: 2024-11-13) |
| Primary citation | Rennie, M.L.,Doolan, A.M.,Raston, C.L.,Crowley, P.B. Protein Dimerization on a Phosphonated Calix[6]arene Disc. Angew. Chem. Int. Ed. Engl., 56:5517-5521, 2017 Cited by PubMed Abstract: Complex formation between cationic cytochrome c and the water-soluble, poly-anionic p-phosphonatocalix[6]arene (pclx ) was investigated. A crystal structure (at 1.8 Å resolution) revealed a remarkable dimeric disc of pclx that acts like glue to mediate a symmetric (C ) protein dimer. The calixarene disc has a diameter of about 1.5 nm and masks about 360 Å 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 K in the low micromolar range was determined for the charge-rich protein-calixarene complex. In contrast to p-sulfonatocalix[4]arene, the larger pclx has a single, well-defined binding site that mediates the assembly of cytochrome c in solution. PubMed: 28407337DOI: 10.1002/anie.201701500 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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