Baltimore, MD (9/15/98)- New X-ray crystallographic
studies have revealed the working of adenosine triphosphate synthase, the
basis of energy transport in all living organisms.
ATP captures the chemical energy released by the combustion of nutrients
and transfers it to reactions that require energy, e.g. the building up
of cell components, muscle contraction, transmission of nerve messages
and many other functions. ATP synthase molecules located within mitochondria
stick out on the mitochondria, attached to their inner surfaces in mushroom-like
clusters. When food is broken down or metabolized for energy, the last
stages of the process occur within the mitochondria.
The ATP synthase molecule, has two parts. Recently, scientists in Japan
discovered that one part, the "mushroom stem," apparently rotates within
the "mushroom cap." Last year, a Nobel prize was awarded to the researcher
(Paul Boyer, Ph.D., UCLA) who suggested that forming ATP was somehow tied
to this rotation, and the prize was shared with another researcher (John
Walker, Ph.D., Medical Research Council Laboratory, Cambridge, England)
whose team laid out one of two possible structures for the "cap," which
is believed to be short-lived.
In
new research, researchers at Johns Hopkins University determined the other
structure, believed to be the most common form, in living organisms. The
ATP synthase "mushroom cap," they found, contains three identical areas,
arranged like a coil, where ATP is made. Each area is occupied with a different
stage in ATP production.
As the "stem" rotates, it creates a powerful internal shifting in each
of the three coiled sections within the cap. This shifting provides the
energy to cause chemical changes. At one site, the "ingredients" for ATP
come together. At another site, they assemble as ATP, and at the third
site, the rotation readies the fully formed ATP to pop off the synthase
molecule, for use throughout the cell.
A team led by L. Mario Amzel, Ph.D., and Peter Pedersen, Ph.D. used
X-ray crystallography to reveal the molecular structure of adenosine triphosphate
synthase. Inside, the molecule whirls around several times a second while
it triggers production of ATP.
"It's one of the most complex molecules ever revealed, almost six times
larger than the blood molecule hemoglobin," says Pedersen. It's also, the
researchers agree, one of the tiniest and most powerful motors ever identified.
The researchers captured the image of the ATP synthase cap while all
of its sites were in some stage of making ATP, which is essential for the
constant recycling of its precursors. Without this recycling, Pedersen
says, "people would have to produce more than half their body weight in
ATP every day to meet their energy needs."
Some scientists have speculated that the same "free radicals" that damage
skin in aging or cause mutations also might damage mitochondria. "If ATP
synthase is a site of free radical damage, that could explain why we become
less energetic with age," Pedersen says. Now that we know the molecular
structures, we can pinpoint damaged regions if they occur."
The research appears in the current issue of the Proceedings of the
National Academy of Sciences.
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