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The structure of an Organic Lake Phycodnavirus rhodopsin II (OLPVRII), which is a unique protein found in the genome of giant viruses, has been determined thanks to the work of MIPT graduates and Ph.D. students. The paper was published in Nature Communications.
The study is the result of a collaboration that included many MIPT alumni. Dmitry Bratanov was among them. Dmitry, who currently works at the Institute of Complex Systems (ICS-6) at the Research Center Juelich, Germany, says that although viral rhodopsins were first discovered in the so-called giant viruses several years ago, their structure, function, and biological role have remained unclear until now.
Virus - Virus - Size - Bacterium - Microscope
A giant virus is a very large virus, the size of a typical bacterium. It is so big that it is visible under a light microscope. Giant viruses infect green algae, which produce oxygen and help maintain the natural ecological balance of the world's ocean. Therefore, giant viruses are of considerable research interest from an environmental perspective.
"In this work, we deciphered the high-resolution structure of OLPVRII, functionally characterized the protein, and showed that it forms pentamers not only in crystals but in lipid membranes as well," explains Dmitry. "This was no easy task. Numerous experiments had to be performed, for some of them we used sophisticated techniques and equipment. What we have achieved is the result of the hard and meticulous work of the international group of scientists."
Organization - Rhodopsins - Instance - Sodium - Pump
This pentameric organization has previously been observed in some other rhodopsins, such as, for instance, in the light-driven sodium pump KR2. However, what makes the OLPVRII structure peculiar is that it has an unusual pore in the center (see figure 1). Its function remains unknown.
"We think that perhaps the pore acts as an ion channel, most probably for chloride ions," says Kirill Kovalev, a co-author of the paper and Ph.D. student...
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