6TR1

Native cytochrome c6 from Thermosynechococcus elongatus in space group H3

Summary for 6TR1

• Entry DOI: 10.2210/pdb6tr1/pdb
• Descriptor: Cytochrome c6, HEME C, SODIUM ION, ... (6 entities in total)
• Functional Keywords: photosystem i, heme, cyanobacteria, electron transport, photosynthesis
• Biological source: Thermosynechococcus elongatus (strain BP-1); More
• Total number of polymer chains: 3
• Total formula weight: 29515.66

Authors

Falke, S.,Feiler, C.G.,Sarrou, I. (deposition date: 2019-12-17, release date: 2019-12-25, Last modification date: 2024-01-24)

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

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: 32880593
DOI: 10.1107/S2053230X20010249

Experimental method

X-RAY DIFFRACTION (1.7 Å)