2n18

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Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidaseDominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase

Structural highlights 2n18 is a 3 chain structure with sequence from Baker's yeast. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , Related: 1s6v Gene: CCP1, CCP, CPO, YKR066C (Baker's yeast), CYC1, YJR048W, J1653 (Baker's yeast) Activity: Cytochrome-c peroxidase, with EC number 1.11.1.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [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 The complex of yeast cytochrome c peroxidase and cytochrome c is a paradigm of the biological electron transfer (ET). Building on seven decades of research, two different models have been proposed to explain its functional redox activity. One postulates that the intermolecular ET occurs only in the dominant, high-affinity protein-protein orientation, while the other posits formation of an additional, low-affinity complex, which is much more active than the dominant one. Unlike the high-affinity interaction-extensively studied by X-ray crystallography and NMR spectroscopy-until now the binding of cytochrome c to the low-affinity site has not been observed directly, but inferred mainly from kinetics experiments. Here we report the structure of this elusive, weak protein complex and show that it consists of a dominant, inactive bound species and an ensemble of minor, ET-competent protein-protein orientations, which summarily account for the experimentally determined value of the ET rate constant. The low-affinity complex of cytochrome c and its peroxidase.,Van de Water K, Sterckx YG, Volkov AN Nat Commun. 2015 May 6;6:7073. doi: 10.1038/ncomms8073. PMID:25944250 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c peroxidase

spinqualitylabelsall models 2n18, 15 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image