6TSY
Cytochrome c6 from Thermosynechococcus elongatus in a monoclinic space group
Summary for 6TSY
| Entry DOI | 10.2210/pdb6tsy/pdb |
| Descriptor | Cytochrome c6, HEME C, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | cyanobacteria, heme, electron transport, photosystem i, photosynthesis |
| Biological source | Thermosynechococcus elongatus BP-1 |
| Total number of polymer chains | 6 |
| Total formula weight | 58931.28 |
| Authors | Feiler, C.G.,Falke, S.,Sarrou, I. (deposition date: 2019-12-21, release date: 2020-01-15, Last modification date: 2024-10-23) |
| Primary citation | Falke, S.,Feiler, C.,Chapman, H.,Sarrou, I. Crystal structures of native cytochrome c6from Thermosynechococcus elongatus in two different space groups and implications for its oligomerization. Acta Crystallogr.,Sect.F, 76:444-452, 2020 Cited by PubMed Abstract: Native cytochrome c was purified from an extract of strain BP-1 of the thermophilic cyanobacterium Thermosynechococcus elongatus. The protein was crystallized, and with only slight modifications of the buffer and vapour-diffusion conditions two different space groups were observed, namely H3 and C2. Both crystal structures were solved; they contained three and six molecules per asymmetric unit and were refined to 1.7 and 2.25 Å resolution, respectively. To date, the structure of native cytochrome c from T. elongatus has only been reported as a monomer using NMR spectroscopy, i.e. without addressing putative oligomerization, and related structures have only previously been solved using X-ray crystallography after recombinant gene overexpression in Escherichia coli. The reported space groups of related cyanobacterial cytochrome c structures differ from those reported here. Interestingly, the protein-protein interfaces that were observed utilizing X-ray crystallography could also explain homo-oligomerization in solution; specifically, trimerization is indicated by infra-red dynamic light scattering and blue native gel electrophoresis in solution. Trimers were also detected by mass spectrometry. Furthermore, there is an indication of post-translational methylation in the crystal structure. Additionally, the possibility of modifying the crystal size and the redox activity in the context of photosynthesis is shaping the investigated cytochrome as a highly suitable model protein for advanced serial crystallography at highly brilliant X-ray free-electron laser sources. PubMed: 32880593DOI: 10.1107/S2053230X20010249 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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