3cxh

Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a minimal core interface for electron transfer.

spinqualitylabelsall models 3cxh, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cxh is a 20 chain structure with sequence from Mus musculus and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: 6PH, 7PH, 8PE, 9PE, CN6, FES, FRU, GLC, HEM, M3L, PRD_900003, SMA, UMQ Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function QCR1_YEAST Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. COR1 may mediate formation of the complex between cytochromes c and c1. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed In cellular respiration, cytochrome c transfers electrons from cytochrome bc(1) complex (complex III) to cytochrome c oxidase by transiently binding to the membrane proteins. Here, we report the structure of isoform-1 cytochrome c bound to cytochrome bc(1) complex at 1.9 A resolution in reduced state. The dimer structure is asymmetric. Monovalent cytochrome c binding is correlated with conformational changes of the Rieske head domain and subunit QCR6p and with a higher number of interfacial water molecules bound to cytochrome c(1). Pronounced hydration and a "mobility mismatch" at the interface with disordered charged residues on the cytochrome c side are favorable for transient binding. Within the hydrophobic interface, a minimal core was identified by comparison with the novel structure of the complex with bound isoform-2 cytochrome c. Four core interactions encircle the heme cofactors surrounded by variable interactions. The core interface may be a feature to gain specificity for formation of the reactive complex. Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer.,Solmaz SR, Hunte C J Biol Chem. 2008 Jun 20;283(25):17542-9. Epub 2008 Apr 4. PMID:18390544 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome bc1 3D structures

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