6rsj

Cytochrome c co-crystallized with 20 eq. sulfonato-calix[8]arene and soaked with 25 eq. spermine - structure I

spinqualitylabelsall models 6rsj, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rsj is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.27Å Ligands: GOL, HEC, SO4, SPM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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 ( approximately 13 kDa), calix[8]arene ( approximately 1.5 kDa), and effector ( approximately 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. Tuning Protein Frameworks via Auxiliary Supramolecular Interactions.,Engilberge S, Rennie ML, Dumont E, Crowley PB ACS Nano. 2019 Sep 24;13(9):10343-10350. doi: 10.1021/acsnano.9b04115. Epub 2019 , Sep 10. PMID:31490058 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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