samples
crystallized
removing
tag
thrombin
generated
four-residue
gly
ser
met
peptide
n-terminal
native
asp5
residue
based
appl1
bar-ph
crystal
structure
find
general
ph
domain
more
conserved
bar
domain
most
highly
conserved
positions
located
closer
bar
ph
interface
rather
central
region
symmetric
dimerdetermined
crystal
structure
full-length
sv40
st
complex
full-length
subunit
pp2a
structure
reveals
two
novel
zinc-binding
motifs
formed
unique
c-terminal
domain
structural
linkage
unique
domain
st
interaction
site
st
structural
subunit
together
biochemical
data
provide
structural
basis
understanding
tumorigenic
activity
st
protein
crystal
structure
complex
determined
combination
molecular
replacement
using
pp2a
subunit
structure
searching
model
single-wavelength
anomalous
dispersion
intrinsic
zinc
atoms
st
refined
resolution
table
secondary
structures
determined
crystal
structure
indicated
above
aligned
sequences
solid
empty
stars
indicate
residues
interacting
pp2a
subunit
using
side-chain
main-chain
respectively
solid
empty
squares
represent
residues
involved
interactions
between
domain
unique
domain
side-chain
main-chain
atoms
respectively
structural
comparison
a-st
crystal
structure
previously
reported
crystal
structures
ac
complex
a-b56-c
complexes
25,26,45,46
also
support
conclusion
heat
repeats
heat
repeats
form
two
relatively
rigid
blocks
however
substantial
structural
flexibility
between
two
structural
blocks
due
result
accumulative
conformational
changes
heat
repeats
figures
s1
s2
report
crystal
structure
sv40
st
complex
murine
pp2a
subunit
striking
four
a-st
complexes
asymmetric
unit
crystal
lattice
essentially
structure
except
flexible
heat
repeats
subunit
involved
a-st
interaction
observation
argues
strongly
st
structure
well
a-st
interface
observed
crystal
structure
independent
crystal
packing
physiologically
relevant
st
crystal
structure
instead
forming
binuclear
cluster
two
zinc
ions
located
two
separate
positions
form
two
novel
zinc-binding
motifs
first
second
cysteine
clusters
residues
respectively
form
two
zinc-binding
motifs
together
conserved
cys103
his122
respectively
both
zinc
ions
interact
helix
stabilize
structure
c-terminal
unique
domain
however
first
zinc-binding
motif
interact
subunit
pp2a
crystal
structure
instead
crystal
structure
suggests
first
zinc-binding
motif
may
directly
interact
subunit
near
active
site
since
first
zinc-binding
motif
spatially
close
active
site
pp2a
subunit
structural
superposition
pp2a
a-st
complexes
figure
addition
inhibition
phosphatase
activity
pp2a
ac
dimer
domain
may
also
play
role
oncogenic
activity
st
providing
additional
binding
site
hsp70
even
complex
pp2a
ac
complex
suggested
crystal
structure