1L0N
native structure of bovine mitochondrial cytochrome bc1 complex
Summary for 1L0N
| Entry DOI | 10.2210/pdb1l0n/pdb |
| Descriptor | UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, Ubiquinol-cytochrome C reductase complex 7.2 kDa protein, cytochrome b-c1 complex 6.4K protein, ... (13 entities in total) |
| Functional Keywords | cytochrome bc1, membrane protein, heme protein, iron sulfur protein, cytochrome b, cytochrome c1, mitochondrial processing protease, mpp, oxidoreductase |
| Biological source | Bos taurus (cattle) More |
| Cellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P31800 P23004 Mitochondrion inner membrane: P00130 P07552 P13272 P00129 P13271 P00126 P13272 Mitochondrion inner membrane; Multi-pass membrane protein (By similarity): P00157 Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side: P00125 |
| Total number of polymer chains | 11 |
| Total formula weight | 243099.42 |
| Authors | |
| Primary citation | Gao, X.,Wen, X.,Yu, C.A.,Esser, L.,Tsao, S.,Quinn, B.,Zhang, L.,Yu, L.,Xia, D. The Crystal Structure of Mitochondrial Cytochrome bc1 in Complex with Famoxadone: The Role of Aromatic-Aromatic Interaction in Inhibition Biochemistry, 41:11692-11702, 2003 Cited by PubMed Abstract: Ubiquinol cytochrome c oxido-reductase (EC. 1.10.2.2, bc1) is an integral membrane protein complex essential to cellular respiration. Structures of the 11-subunit mitochondrial bc1 complex were determined with and without the fungicide famoxadone. Specific inhibition by famoxadone is achieved through a coordinated optimization of aromatic-aromatic interactions where conformational rearrangements in famoxadone and in residues lining the inhibitor-binding pocket produce a network of aromatic-aromatic interactions that mimic the crystal lattice of benzene. The profound aromatic-aromatic interactions as supported by prior mutagenesis provide a structural basis for specific protein-ligand interaction in a hydrophobic environment. Dramatic conformational changes, both in cyt. b and ISP subunits in the inhibitor-protein complex, confer experimental evidence for a functional role of cytochrome b in the induced conformational arrest of ISP and allow the identification of a possible intrasubunit signal transduction pathway that controls the movement of ISP. These results support an inhibitory mechanism that is consistent with the requirement for ISP movement in the electron transfer of this complex. PubMed: 12269811DOI: 10.1021/bi026252p PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
