3h1j

Stigmatellin-bound cytochrome bc1 complex from chicken

spinqualitylabelsall models 3h1j, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3h1j is a 20 chain structure with sequence from Gallus gallus. The May 2011 RCSB PDB Molecule of the Month feature on Cytochrome bc1 by David Goodsell is 10.2210/rcsb_pdb/mom_2011_5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CDL, FES, GOL, HEC, HEM, PEE, PLC, SMA, UNL, UQ NonStd Res: UNK Related: 2bcc, 2pp9, 1sqx, 3cx5, 3h1h, 3h1i, 3h1k, 3h1l Activity: Ubiquinol--cytochrome-c reductase, with EC number 1.10.2.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CYB_CHICK] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (By similarity). [UCRI_CHICK] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The cytochrome bc1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron-sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe-S protein by ubiquinol. The other site is close enough to cytochrome c1 to allow oxidation of the Fe-S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe-S component in order to shuttle electrons from ubiquinol to cytochrome c1. Such a mechanism has not previously been observed in redox protein complexes. Electron transfer by domain movement in cytochrome bc1.,Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH Nature. 1998 Apr 16;392(6677):677-84. PMID:9565029 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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