3T6E
Crystal Structure of the Reaction Centre from Blastochloris viridis strain DSM 133 (ATCC 19567) substrain-94
Summary for 3T6E
| Entry DOI | 10.2210/pdb3t6e/pdb |
| Related | 1DXR 1PRC 1VRN 2I5N 2JBL 2WJM 2WJN 3T6D |
| Descriptor | Photosynthetic reaction center cytochrome c subunit, GLYCEROL, BACTERIOCHLOROPHYLL B, ... (17 entities in total) |
| Functional Keywords | pigment-protein complex, electron transfer, photosynthesis, photosynthetic reaction center, photosynthetic membranes, evolution, genetic drift, electron transport |
| 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 | 158882.31 |
| Authors | Roszak, A.W.,Gardiner, A.T.,Isaacs, N.W.,Cogdell, R.J. (deposition date: 2011-07-28, release date: 2011-11-23, Last modification date: 2024-10-16) |
| Primary citation | Roszak, A.W.,Moulisova, V.,Reksodipuro, A.D.,Gardiner, A.T.,Fujii, R.,Hashimoto, H.,Isaacs, N.W.,Cogdell, R.J. New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory. Biochem.J., 442:27-37, 2012 Cited by PubMed Abstract: Newly determined crystal structures of the photosynthetic RC (reaction centre) from two substrains of the non-sulfur purple bacterium Blastochloris viridis strain DSM 133, together with analysis of their gene sequences, has revealed intraspecies evolutionary changes over a period of 14 years. Over 100 point mutations were identified between these two substrains in the four genes encoding the protein subunits of the RC, of which approximately one-fifth resulted in a total of 16 amino acid changes. The most interesting difference was in the M subunit where the change from a leucine residue to glycine in the carotenoid-binding pocket allowed NS5 (1,2-dihydroneurosporene) to adopt a more sterically favoured conformation, similar to the carotenoid conformation found in other related RCs. The results of the present study, together with a high rate of mutations in laboratory bacterial cultures described recently, suggest that bacteria evolve faster than has been generally recognized. The possibility that amino acid changes occur within protein sequences, without exhibiting any immediately observable phenotype, should be taken into account in studies that involve long-term continuous growth of pure bacterial cultures. The Blc. viridis RC is often studied with sophisticated biophysical techniques and changes such as those described here may well affect their outcome. In other words, there is a danger that laboratory-to-laboratory variation could well be due to different groups not realising that they are actually working with slightly different proteins. A way around this problem is suggested. PubMed: 22054235DOI: 10.1042/BJ20111540 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.92 Å) |
Structure validation
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