Researchers from the Pacific Northwest National Laboratory and Brookhaven National Laboratory in the United States have determined the crystal structure of a protein cce_0566, which is labeled DUF269, from a photosynthetic bacterium with a completely different lifestyle during the day and night photosynthetic bacterium) cyanobacteria 51142, and it also belongs to a family of proteins containing an unknown functional domain.
They found that a crack achievable by a solvent containing conservatively charged amino acid residues at the interface of the asymmetric unit of the crystal may be an active site or ligand binding surface. The protein folding observed in Cyanothece 51142 appears to be unique to the DUF269 protein family.
In the daytime, cyanobacteria 51142 uses sunlight to convert carbon dioxide into molecular oxygen and glucose, a process known as photosynthesis. At night, it uses glucose to convert nitrogen in the atmosphere into bioavailable ammonia, a process known as nitrogen fixation.
Understanding how this single-celled organism regulates photosynthesis and nitrogen fixation may be of great benefit to multicellular organisms such as humans, because hydrogen is a byproduct of nitrogen fixation. The clues to understanding the process of regulating nitrogen fixation may exist in 34 genes in the nitrogen fixation gene collection of cyanobacteria. DUF269 is one of these genes.
The cce_0566 crystal was cultivated at the Pacific Northwest National Laboratory and sent to Brookhaven National Laboratory for X-ray diffraction experiments. Nuclear magnetic resonance data and other biophysical data confirmed that the biological unit of DUF269 in solution was the same as that observed in the asymmetric unit of the dimer crystal.
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