How does ATP couple endergonic and exergonic reactions?

The question is a bit misleading - ATP gets endergonic reactions to

work because
it is an exergonic reaction itself, and
it couples itself to the endergonic reaction, so that the overall
reaction is exergonic.
Exergonic reactions are spontaneous reactions. That is, they are
thermodynamically favoured - G < 0. The problem for the body
comes when a desired reaction is endergonic - i.e. non-spontanous.
In the normal state of affairs, such a reaction never takes place. Yet
many essential reactions are endergonic. How does the body
sidestep the problem?
The body's ingenious solution is to use another exergonic process to
drive the non-spontaneous (endergonic) one. More accurately, it
couples the exergonic reaction with the endogonic one so that the
free energy released from the former reaction propels the latter one.
For its chosen exergonic reaction, the body generally uses the
hydrolysis of ATP (adenosine triphosphate). This is the major
'energy' molecule produced by metabolism, and it serves as a sort
of 'energy shuttle': ATP is dispatched to wherever an endergonic
reaction needs to take place, and the two reactions are coupled so
that the overall reaction is thermodynamically favoured.
To make this more concrete, let's look at the synthesis of Glutamine.
This molecule is produced in the following manner:
Glutamic acid + Ammonia Glutamine
Unfortunately, this reaction is non-spontaneous (G = +3.4
kcal/mol). However, ATP is at hand. The hydrolysis of ATP (ATP +
H2O ADP + Pi) is highly exergonic - (G = -7.3). As you can see if
these reactions could somehow be coupled, together the overall
reaction would be favoured: G would be -3.9. And so, with the help
of ATP, the body can synthesise glutamine without breaking any
thermodynamic laws.
But to return to our original question, how exactly is this coupling
achieved? The basic answer is this: when ATP is hydrolysed, the free
phosphate group (Pi) isn't wasted. Instead, it is transferred to some
other molecule, such as the reactant. The molecule is thus
phosphorylated. However, this phosphorylated molecule is thereby
rendered unstable - it is 'keen' to react all of a sudden. And this newfound tendency allows the desired reaction to take place.

To help make this clearer, I've drawn a diagram of the Glutamic acid
+ Ammonia Glutamine reaction above. The big blue molecule is
glutamic acid; the other players in the drama are labelled.

In the first stage, the reactants are in place, but since the reaction is
non-spontaneous, they are powerless to get going. ATP arrives to
help out.
In the second stage, ATP is hydrolysed to ADP + Pi. However, the
phosphate group binds to the glutamic acid molecule
(phosphorylates it). This phosphorylated intermediate is more
reactive than the glutamic acid was by itself.
In the final stage, the ammonia group displaces the phosphate one.
This reaction is spontaneous, thanks to the phosphate group making
the complex in stage 2 more unstable. Thus, ATP allows glutamine
to be formed via two spontaneous reactions, but the price to be paid
is that the ATP molecule has been used up - it has been hydrolysed
to ADP and Pi.
There are many other examples of ATP's action, but in almost all
cases a substance is phosphorylated. As always, this
phosphorylated intermediate is more reactive than the original
reactant, and so what was once an endergonic reaction is thus
rendered exeronic by the coupling of the original reaction with the
hydrolysis of ATP