A recent study published in the journal Nature Communications by researchers from Arizona State University details their success at designing the blueprint of diacylglycerol kinase, a cell that is regarded as fundamental to the functioning of other body cells and therefore called the “nanomachine” by scientists.
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The team of scientists was able to rely on the X-ray free-electron laser located at Stanford Linear Accelerator Center – the brightest source of X-ray on Earth, without which the experiment might not have been possible. The success of the experiment has enabled scientists to attend to questions that had been left unanswered for 50 years about the roles and mechanisms of this tiny enzyme.
Diacylglycerol kinase is very fundamental to metabolic activities as well as cell functions, and it helps with protein regulation, secretory needs, and cellular transport among other cellular functions that give life and health. This tiny enzyme has also been fingered in energy transfer from some molecules to certain substrates, influencing their actions and purpose at binding with other molecules.
Not only this, kinase was also discovered to impact on the synthesis of bacterial cell wall. Scientists have now obtained insights into how this cell membrane activity operates.
"How this diminutive nanomachine, less than 10 nm tall, brings these two disparate substrates together at the membrane interface for reaction is revealed in a molecularly detailed crystal structure,” said Professor of Membrane Structural and Functional Biology at Trinity College Dublin, Martin Caffrey.
“It is the smallest known kinase, and seeing its form with crystal clarity is now helping us to answer questions that formed from over 50 years of work on this paradigmatic protein," Caffrey added.
The X-ray free-electron laser at Stanford enabled researchers to fully observe how this tiny enzyme functions at the molecular level, and to this end, Professor Caffrey disclosed that the Stanford X-ray machine gives off bursts of X-rays that are a quad-trillionth of a second long in duration, and this enabled the team of scientists to map the structural details of the enzyme long before it vaporized through radiation damage via what the team calls “Hit-and-Run serial crystallography.”
The director of the Center for Applied Structural Discovery at Arizona State University's Biodesign Institute, Petra Fromme, noted that this study provided the team with the first opportunity to obtain the “structure of a protein that is a membrane-integral enzyme and important biocatalyst in the cell,” and this is against the fact that biocatalysts increase the speed at which crucial biological events take place in the body.
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The National Institutes of Health funded some of the projects of the Center for Membrane Proteins in Infectious Diseases at the Arizona State University to investigate kinase, and ASU to this end had been committed to understanding the molecular basis by which bacterial and viral proteins functional in diseases have been teaming up with natural proteins in the body to ward off pathogen attacks.