Figure S1
PHYRE2
HHrepIDFigure S1. Secondary structure prediction of CmTic110.
Secondary structure prediction was performed using PHYRE2. CmTic110 is
predicted to have an all α-helices structure and the predicted α -helical regions are
marked as green tubes under the sequence. The HEAT repeat regions predicted
by HHrepID are indicated as magenta tubes below the PHYRE2 secondary
structure prediction.900
900
Figure S2
(c)
Figure S2. Putative oligomerization of CmTic110C.
(a) CmTic110C extended into a super-helical structure in crystal packing. For clarity, only the C
α backbone of the molecules is shown. Each monomer is colored with green or blue.
(b) The head-to-head and tail-to-tail dimers were fitted with the scattering data with CRYSOL
with the χ value shown. The structures are shown in cartoon with A subunit in green and B
subunit in cyan.
(b) Combining the SAXS envelopes of CmTic110B (cyan) and CmTic110C (green) and the
crystal structure of the tail-to-tail dimer of CmTic110C. The envelopes and structure are
superimposed using the program SUPCOMB.
head dimer1
0 0.1 0.2 0.3 0.4
q(Å-1)
I(q
) χ= 8.308
CmTic110C
CRYSOL
(b)
900
900
(a)
head-to-headdimer
t aildimer
0 0.1 0.2 0.3 0.4
q(Å-1)
I(q
)
χ= 6.412
CmTic110C
CRYSOL
tail-to-taildimer
10-1
10-2
10-3
10-4
10-5
10-1
10-2
10-3
10-4
10-5Figure S3
(a)
1.8
1.6
1.4
1.2
1.0
0.8
30
25
15
10
  5
  0
20
1 10 100 1000 104 105
Time (µs)
A
ut
oc
or
re
la
tio
n
 %
 In
te
ns
ity
1 10 100 10000.1
Radius (nm)
1.8
1.6
1.4
1.2
1.0
0.8
50
40
30
20
10
  0
1 10 100 1000 104 105
Time (µs)
A
ut
oc
or
re
la
tio
n
 %
 In
te
ns
ity
1 10 100 10000.1
Radius (nm)
(b)
CmTic110B CmTic110B
CmTic110C CmTic110C
Figure S3. Dynamic light scattering measurements of CmTic110B and CmTic110C.
(a) and (b) Left panels show the intensity autocorrelation function of CmTic110B
and CmTic110C, respectively, measured by dynamic light scattering (filled circles)
and the data fitting by the cumulant expansion (open circles). Size distributions of
particles extracted from the autocorrelation function of both proteins are shown in
the right panels. The calculated Stokes radius is 73 Å for CmTic110B and 50 Å for
CmTic110C.Figure S4
Sra1
Cul4A
Nup107
Cul1
(a)
(b)
(c)
(d)
Figure S4. Proteins with high structural homology to CmTic110C identified by
DALI. Structures on the left are structures of the proteins identified by DALI. The
colored region is aligned to CmTic110C. Structures on the right are
superimpositions with CmTic110C (green).
(a) Sra1 in the WAVE regulatory complex (3p8c).
(b) Cullin Cul4Ain the damage-specific DNA binding protein 1 (DDB1)-Cul4A-
Roc1-SV5-V complex (2hye).
(c)Nuclear pore complex protein Nup107 (3i4r).
(d) Cullin Cul1 in the Cul1-Rbx1-Skp1-F boxSkp2complex (1ldj).Figure S5
50 amino  acid Predicted HEAT
Repeat
Observed HEAT repeat in crystal
structure
PsTic110
CmTic110
Figure S5. HEAT repeat prediction of pea Tic110 (PsTic110) and CmTic110 using
HHrepID.
Domain coloring is the same as Figure 1a. The HEAT repeats are presented as
blue diamonds above each protein. The four HEAT repeats observed in our
structure are presented as green diamonds below CmTic110.