2FYU
Crystal structure of bovine heart mitochondrial bc1 with jg144 inhibitor
Summary for 2FYU
| Entry DOI | 10.2210/pdb2fyu/pdb |
| Related | 1L0L 1L0N 1QCR 1SQV 1SQX |
| Descriptor | Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial, Ubiquinol-cytochrome c reductase complex 7.2 kDa protein, Ubiquinol-cytochrome c reductase complex 6.4 kDa protein, ... (15 entities in total) |
| Functional Keywords | transmembrane helices, 11 protein complex, oxidoreductase |
| Biological source | Bos taurus (cattle) More |
| Cellular location | Mitochondrion inner membrane; Peripheral membrane protein; Matrix side: P31800 P00125 Mitochondrion inner membrane: P00130 P07552 P23004 P00157 P13271 P00126 P13272 Mitochondrion inner membrane; Multi-pass membrane protein (By similarity): P13272 Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side: P00129 |
| Total number of polymer chains | 11 |
| Total formula weight | 243636.98 |
| Authors | |
| Primary citation | Esser, L.,Gong, X.,Yang, S.,Yu, L.,Yu, C.A.,Xia, D. Surface-modulated motion switch: Capture and release of iron-sulfur protein in the cytochrome bc1 complex. Proc.Natl.Acad.Sci.Usa, 103:13045-13050, 2006 Cited by PubMed Abstract: In the cytochrome bc(1) complex, the swivel motion of the iron-sulfur protein (ISP) between two redox sites constitutes a key component of the mechanism that achieves the separation of the two electrons in a substrate molecule at the quinol oxidation (Q(o)) site. The question remaining is how the motion of ISP is controlled so that only one electron enters the thermodynamically favorable chain via ISP. An analysis of eight structures of mitochondrial bc(1) with bound Q(o) site inhibitors revealed that the presence of inhibitors causes a bidirectional repositioning of the cd1 helix in the cytochrome b subunit. As the cd1 helix forms a major part of the ISP binding crater, any positional shift of this helix modulates the ability of cytochrome b to bind ISP. The analysis also suggests a mechanism for reversal of the ISP fixation when the shape complementarity is significantly reduced after a positional reorientation of the reaction product quinone. The importance of shape complementarity in this mechanism was confirmed by functional studies of bc(1) mutants and by a structure determination of the bacterial form of bc(1). A mechanism for the high fidelity of the bifurcated electron transfer is proposed. PubMed: 16924113DOI: 10.1073/pnas.0601149103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
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