6GDA
Cytochrome c in complex with Sulfonato-calix[8]arene, P43212 form soaked with Spermine
Summary for 6GDA
| Entry DOI | 10.2210/pdb6gda/pdb |
| Related | 6GD6 6GD7 6GD8 6GD9 |
| Descriptor | Cytochrome c iso-1, HEME C, sulfonato-calix[8]arene, ... (6 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 | 18397.96 |
| Authors | Rennie, M.L.,Fox, G.C.,Crowley, P.B. (deposition date: 2018-04-23, release date: 2019-05-01, Last modification date: 2024-01-17) |
| Primary citation | Engilberge, S.,Rennie, M.L.,Dumont, E.,Crowley, P.B. Tuning Protein Frameworks via Auxiliary Supramolecular Interactions. Acs Nano, 13:10343-10350, 2019 Cited by PubMed Abstract: Protein crystals with their precise, periodic array of functional building blocks have potential applications in biomaterials, sensing, and catalysis. This paper describes how a highly porous crystalline framework of a cationic redox protein and an anionic macrocycle can be modulated by a small cationic effector. Ternary composites of protein (∼13 kDa), calix[8]arene (∼1.5 kDa), and effector (∼0.2 kDa) formed distinct crystalline architectures, dependent on the effector concentration and the crystallization technique. A combination of X-ray crystallography and density functional theory (DFT) calculations was used to decipher the framework variations, which appear to be dependent on a calixarene conformation change mediated by the effector. This "switch" calixarene was observed in three states, each of which is associated with a different interaction network. Two structures obtained by co-crystallization with the effector contained an additional protein "pillar", resulting in framework duplication and decreased porosity. These results suggest how protein assembly can be engineered by supramolecular host-guest interactions. PubMed: 31490058DOI: 10.1021/acsnano.9b04115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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