A comparative look at structural variation among RC–LH1 ‘Core’ complexes present in anoxygenic phototrophic bacteria
| Autor: | Richard J. Cogdell, Alastair T. Gardiner, Tu C. Nguyen-Phan |
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| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular Protein Conformation Stereochemistry Photosynthetic Reaction Center Complex Proteins Light-Harvesting Protein Complexes Reaction centres Rhodobacter sphaeroides Review Plant Science medicine.disease_cause Chromatiaceae Biochemistry Structure-Activity Relationship Anoxygenic phototrophs Bacterial Proteins Benzoquinones medicine Roseiflexus castenholzii Photosynthesis Structures Phototroph biology Chemistry Blastochloris viridis Genetic Variation Cell Biology General Medicine biology.organism_classification Anoxygenic photosynthesis Light harvesting Rhodopseudomonas Chloroflexi (class) Energy Transfer RC–LH1 Purple photosynthetic bacteria Photosynthetic bacteria Rhodopseudomonas palustris |
| Zdroj: | Photosynthesis Research |
| ISSN: | 1573-5079 0166-8595 |
| DOI: | 10.1007/s11120-020-00758-3 |
| Popis: | All purple photosynthetic bacteria contain RC–LH1 ‘Core’ complexes. The structure of this complex from Rhodobacter sphaeroides, Rhodopseudomonas palustris and Thermochromatium tepidum has been solved using X-ray crystallography. Recently, the application of single particle cryo-EM has revolutionised structural biology and the structure of the RC–LH1 ‘Core’ complex from Blastochloris viridis has been solved using this technique, as well as the complex from the non-purple Chloroflexi species, Roseiflexus castenholzii. It is apparent that these structures are variations on a theme, although with a greater degree of structural diversity within them than previously thought. Furthermore, it has recently been discovered that the only phototrophic representative from the phylum Gemmatimonadetes, Gemmatimonas phototrophica, also contains a RC–LH1 ‘Core’ complex. At present only a low-resolution EM-projection map exists but this shows that the Gemmatimonas phototrophica complex contains a double LH1 ring. This short review compares these different structures and looks at the functional significance of these variations from two main standpoints: energy transfer and quinone exchange. |
| Databáze: | OpenAIRE |
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