2IBZ
Yeast Cytochrome BC1 Complex with Stigmatellin
Summary for 2IBZ
Entry DOI | 10.2210/pdb2ibz/pdb |
Related | 1EZV 1KB9 1KYO 1P84 |
Descriptor | Ubiquinol-cytochrome-c reductase complex core protein 1, Variable Heavy chain of antibody fragment, Variable Light chain of antibody fragment, ... (16 entities in total) |
Functional Keywords | multisubunit membrane protein complex, oxidoreductase |
Biological source | Mus musculus (house mouse) More |
Cellular location | Mitochondrion inner membrane : P07256 P07257 P00127 P00128 P08525 P22289 Mitochondrion inner membrane ; Multi-pass membrane protein : P00163 Mitochondrion inner membrane; Single-pass membrane protein; Intermembrane side: P07143 Mitochondrion inner membrane ; Single-pass membrane protein : P08067 |
Total number of polymer chains | 11 |
Total formula weight | 249144.47 |
Authors | Hunte, C. (deposition date: 2006-09-12, release date: 2007-03-20, Last modification date: 2024-11-13) |
Primary citation | Lancaster, C.R.,Hunte, C.,Kelley, J.,Trumpower, B.L.,Ditchfield, R. A Comparison of Stigmatellin Conformations, Free and Bound to the Photosynthetic Reaction Center and the Cytochrome bc(1) Complex. J.Mol.Biol., 368:197-208, 2007 Cited by PubMed Abstract: We describe in detail the conformations of the inhibitor stigmatellin in its free form and bound to the ubiquinone-reducing (Q(B)) site of the reaction center and to the ubiquinol-oxidizing (Q(o)) site of the cytochrome bc(1) complex. We present here the first structures of a stereochemically correct stigmatellin in complexes with a bacterial reaction center and the yeast cytochrome bc1 complex. The conformations of the inhibitor bound to the two enzymes are not the same. We focus on the orientations of the stigmatellin side-chain relative to the chromone head group, and on the interaction of the stigmatellin side-chain with these membrane protein complexes. The different conformations of stigmatellin found illustrate the structural variability of the Q sites, which are affected by the same inhibitor. The free rotation about the chi1 dihedral angle is an essential factor for allowing stigmatellin to bind in both the reaction center and the cytochrome bc1 pocket. PubMed: 17337272DOI: 10.1016/j.jmb.2007.02.013 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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