1l0n

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Revision as of 18:01, 20 November 2007

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spinqualitylabelsall models 1l0n, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

native structure of bovine mitochondrial cytochrome bc1 complex

Overview

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.

About this Structure

1L0N is a Protein complex structure of sequences from Bos taurus with HEM and FES as ligands. Active as Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Full crystallographic information is available from OCA.

Reference

The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition., Gao X, Wen X, Yu C, Esser L, Tsao S, Quinn B, Zhang L, Yu L, Xia D, Biochemistry. 2002 Oct 1;41(39):11692-702. PMID:12269811

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