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Structure of a membrane-embedded prenyltransferase homologous to UBIAD1.
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Membrane-embedded
prenyltransferases
from
the
UbiA
family
catalyze
the
Mg
2
+
-
dependent
transfer
of
a
hydrophobic
polyprenyl
chain
onto
a
variety
of
acceptor
molecules
and
are
involved
in
the
synthesis
of
molecules
that
mediate
electron
transport
,
including
Vitamin
K
and
Coenzyme
Q
.
In
humans
,
missense
mutations
to
the
protein
UbiA
prenyltransferase
domain-containing
1
(
UBIAD
1
)
are
responsible
for
Schnyder
crystalline
corneal
dystrophy
,
which
is
a
genetic
disease
that
causes
blindness
.
Mechanistic
understanding
of
this
family
of
enzymes
has
been
hampered
by
a
lack
of
three
-dimensional
structures
.
We
have
solved
structures
of
a
UBIAD
1
homolog
from
Archaeoglobus
fulgidus
,
AfUbiA
,
in
an
unliganded
form
and
bound
to
Mg
2
+
and
two
different
isoprenyl
diphosphates
.
Functional
assays
on
MenA
,
a
UbiA
family
member
from
E
.
coli
,
verified
the
importance
of
residues
involved
in
Mg
2
+
and
substrate
binding
.
The
structural
and
functional
studies
led
us
to
propose
a
mechanism
for
the
prenyl
transfer
reaction
.
Disease-causing
mutations
in
UBIAD
1
are
clustered
around
the
active
site
in
AfUbiA
,
suggesting
the
mechanism
of
catalysis
is
conserved
between
the
two
homologs
.
