3CXH
Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a minimal core interface for electron transfer.
Summary for 3CXH
| Entry DOI | 10.2210/pdb3cxh/pdb |
| Related | 1EZV 1KB9 1KYO 3CX5 |
| Related PRD ID | PRD_900003 |
| Descriptor | Cytochrome b-c1 complex subunit 1, mitochondrial, HEAVY CHAIN (VH) OF FV-FRAGMENT, LIGHT CHAIN (VL) OF FV-FRAGMENT, ... (23 entities in total) |
| Functional Keywords | complex iii, cytochrome c isoform-2, electron transfer complex, cytochrome bc1 complex, mitochondrialtransmembrane complex, respiratory chain, transient protein-protein interaction, electron transport, inner membrane, mitochondrion, transit peptide, transport, phosphoprotein, heme, iron, metal-binding, iron-sulfur, oxidoreductase |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 23 |
| Total formula weight | 533742.33 |
| Authors | Solmaz, S.R.N.,Hunte, C. (deposition date: 2008-04-24, release date: 2008-05-13, Last modification date: 2023-08-30) |
| Primary citation | Solmaz, S.R.,Hunte, C. Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. J.Biol.Chem., 283:17542-17549, 2008 Cited by PubMed Abstract: 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. PubMed: 18390544DOI: 10.1074/jbc.M710126200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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