3G7F
Crystal structure of Blastochloris viridis heterodimer mutant reaction center
Summary for 3G7F
| Entry DOI | 10.2210/pdb3g7f/pdb |
| Descriptor | Photosynthetic reaction center cytochrome c subunit, BACTERIOPHEOPHYTIN B, UBIQUINONE-1, ... (15 entities in total) |
| Functional Keywords | heterodimer mutant, blastochloris viridis, photosynthetic reaction center, membrane protein structure, microfluidics, plugs, cell membrane, electron transport, heme, iron, lipoprotein, membrane, metal-binding, photosynthesis, reaction center, transport, bacteriochlorophyll, chlorophyll, chromophore, formylation, transmembrane, magnesium |
| Biological source | Blastochloris viridis More |
| Cellular location | Cell membrane; Lipid-anchor: P07173 Cellular chromatophore membrane; Single-pass membrane protein: P06008 Cellular chromatophore membrane; Multi-pass membrane protein (By similarity): P06009 P06010 |
| Total number of polymer chains | 4 |
| Total formula weight | 145584.97 |
| Authors | Ponomarenko, N.S.,Li, L.,Tereshko, V.,Ismagilov, R.F.,Norris Jr., J.R. (deposition date: 2009-02-09, release date: 2009-09-22, Last modification date: 2024-11-20) |
| Primary citation | Ponomarenko, N.S.,Li, L.,Marino, A.R.,Tereshko, V.,Ostafin, A.,Popova, J.A.,Bylina, E.J.,Ismagilov, R.F.,Norris, J.R. Structural and spectropotentiometric analysis of Blastochloris viridis heterodimer mutant reaction center Biochim.Biophys.Acta, 1788:1822-1831, 2009 Cited by PubMed Abstract: Heterodimer mutant reaction centers (RCs) of Blastochloris viridis were crystallized using microfluidic technology. In this mutant, a leucine residue replaced the histidine residue which had acted as a fifth ligand to the bacteriochlorophyll (BChl) of the primary electron donor dimer M site (HisM200). With the loss of the histidine-coordinated Mg, one bacteriochlorophyll of the special pair was converted into a bacteriopheophytin (BPhe), and the primary donor became a heterodimer supermolecule. The crystals had dimensions 400 x 100 x 100 microm, belonged to space group P4(3)2(1)2, and were isomorphous to the ones reported earlier for the wild type (WT) strain. The structure was solved to a 2.5 A resolution limit. Electron-density maps confirmed the replacement of the histidine residue and the absence of Mg. Structural changes in the heterodimer mutant RC relative to the WT included the absence of the water molecule that is typically positioned between the M side of the primary donor and the accessory BChl, a slight shift in the position of amino acids surrounding the site of the mutation, and the rotation of the M194 phenylalanine. The cytochrome subunit was anchored similarly as in the WT and had no detectable changes in its overall position. The highly conserved tyrosine L162, located between the primary donor and the highest potential heme C(380), revealed only a minor deviation of its hydroxyl group. Concomitantly to modification of the BChl molecule, the redox potential of the heterodimer primary donor increased relative to that of the WT organism (772 mV vs. 517 mV). The availability of this heterodimer mutant and its crystal structure provides opportunities for investigating changes in light-induced electron transfer that reflect differences in redox cascades. PubMed: 19539602DOI: 10.1016/j.bbamem.2009.06.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report
