6YQ8
Crystal structure of native Phycocyanin from T. elongatus in spacegroup P63 at 1.8 Angstroms
Summary for 6YQ8
| Entry DOI | 10.2210/pdb6yq8/pdb |
| Descriptor | C-phycocyanin alpha chain, C-phycocyanin beta chain, PHYCOCYANOBILIN, ... (7 entities in total) |
| Functional Keywords | native c-phycocyanin, antenna protein, heterodimer, ligand-bound, phycobilisome, chromophore, electron transport, photosynthesis |
| Biological source | Thermosynechococcus elongatus (strain BP-1) More |
| Total number of polymer chains | 2 |
| Total formula weight | 38750.82 |
| Authors | Feiler, C.G.,Falke, S.,Sarrou, I. (deposition date: 2020-04-16, release date: 2021-01-20, Last modification date: 2024-01-24) |
| Primary citation | Sarrou, I.,Feiler, C.G.,Falke, S.,Peard, N.,Yefanov, O.,Chapman, H. C-phycocyanin as a highly attractive model system in protein crystallography: unique crystallization properties and packing-diversity screening. Acta Crystallogr D Struct Biol, 77:224-236, 2021 Cited by PubMed Abstract: The unique crystallization properties of the antenna protein C-phycocyanin (C-PC) from the thermophilic cyanobacterium Thermosynechococcus elongatus are reported and discussed. C-PC crystallizes in hundreds of significantly different conditions within a broad pH range and in the presence of a wide variety of precipitants and additives. Remarkably, the crystal dimensions vary from a few micrometres, as used in serial crystallography, to several hundred micrometres, with a very diverse crystal morphology. More than 100 unique single-crystal X-ray diffraction data sets were collected from randomly selected crystals and analysed. The addition of small-molecule additives revealed three new crystal packings of C-PC, which are discussed in detail. The high propensity of this protein to crystallize, combined with its natural blue colour and its fluorescence characteristics, make it an excellent candidate as a superior and highly adaptable model system in crystallography. C-PC can be used in technical and methods development approaches for X-ray and neutron diffraction techniques, and as a system for comprehending the fundamental principles of protein crystallography. PubMed: 33559611DOI: 10.1107/S2059798320016071 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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