Skip to main content

Table 1 Pks13, Mas and PpsA constructs and their global and hydrodynamic properties

From: Solution structure of the type I polyketide synthase Pks13 from Mycobacterium tuberculosis

Protein a

Pks13 (Holo-Pks13)

Pks13(S1533A) monomer (C16-Pks13(S1533A) dimer)

fACP1‑KS‑AT

fKS‑AT

fKS

fAT

AT52

fACP2‑TE

fTE

Mas monomer (Dimer)

PpsA

Sequence boundaries

1–1733

1–1733

1–1063

119–1071

119–575

591–1046

576–1063

1154–1733

1437–1725

1–2111

1–1876

MWth (kDa), Number of residues

188.0, 1746

188.0, 1746 (376.0, 3492)

115.8, 1084

104.2, 974

50.5, 478

49.2, 479

55.1, 510

63.6, 583

32.8, 295

225.9, 2124 (451.8, 4248)

200.4, 1889

[NaCl] (mM)

50

50

50

50

50

300

300

50

50

50

500

pH

8.0

8.0

8.5

8.0

8.0

8.0

8.0

7.5

8.0

8.0

8.0

10% glycérol

2 mM EDTA

10% glycérol

DLSb

Rh (nm)

7.3 (7.9)

6.9 (8.7)

4.2

4.5

3.4

3.0

3.7

3.4

2.4

6.5 (–)

8.1

Pd (%)

17 (25)

26 (35)

19

23

25

20

15

27

19

13 (–)

18

SAXSc

Rg (nm)

7.4 ± 0.1/7.7 (7.4 ± 0.1/7.6)

8.2 ± 0.4/7.9 (10.3 ± 0.1/10.7± 0.1)

3.8 ± 0.1/4.0

3.8/3.8

2.8 ± 0.1/2.9

2.8 ± 0.0/2.7

3.4 /3.5

3.1/3.4

1.9 ± 0.1/2.0

5.7/5.9 (8.0 ± 0.2/8.4)

6.4 ± 0.3/ 6.5

MW (kDa)

210/214 (248/255)

−/−

105/105

110/110

−/−

−/−

44/44

46/47

26/27

−/−

−/−

−/−

−/−

MWind (kDa)

214 ± 26/190 (216 ± 22/179)

227 ± 30/227 (431 ± 36/290)

116 ± 7/125

102 ± 2/115

54 ± 7/58

54 ± 6/60

58 ± 3/64

59 ± 1/63

27 ± 3/30

221 ± 23/225 (334 ± 99 /343 )

182 ± 16/217

Dmax (nm)

24.8 (24.8)

25.0 (36.0)

12.7

13.0

10.0

8.0

12.0

12.0

5.5

21.0 (29.0)

20.2

Oligom. state

M (M)

M (D)

M

M

M

M

M

M

M

M (D)

M

tRg (nm) d

3.8/4.9/13.9

3.8/4.9/13.9

3.1/4.1/ 10.9

3.0/3.9/10.3

2.3/3.0/7.2

2.3/3.0/7.3

2.3/3.0/7.3

2.5/3.2/8.0

1.9/2.5/5.6

4.0/5.3/13.9

3.9/5.0/14.4

χ DAMMIN/ GASBOR/

Comparison with HR model

1.36/2.69/3.11 (−/−/−)

1.16/−/− (1.16/−/−)

1.80/2.80/1.02

1.57/1.83/1.36

1.28/1.10/1.11

2.91/2.72/1.14

2.12/2.68/3.10

1.86/4.32/1.97

3.41/2.93/1.67

1.44/1.54/−

1.32/1.56/−

  1. a Theoretical molecular weight and number of residues given for the tagged proteins in the case of Pks13, holo-Pks13, C16-Pks13(S1533A), Mas, PpsA, fACP1‑KS‑AT, fKS‑AT, fKS, fAT, AT52 and after removal of the His6-tag for fACP2‑TE and fTE
  2. b Hydrodynamic radii (Rh) and percentage of polydispersity obtained from dynamic light scattering at 20 °C. Histograms of Rh can be found in Additional file 1: Table S1
  3. cRg, gyration radii based on Guinier plot/distance distribution function. MW, molecular weight based on I0 from Guinier plot/I0 from distance distribution function p(r). MWind, molecular weight based on the concentration-independent methods by Rambo and Tainer/SAXSMoW calculator. Dmax maximum dimension. Oligomeric state (monomer, M; partial dimerization, D) obtained from SAXS (at 12–15 °C). For data arising from online HPLC measurements, only the concentration-independent evaluation of the molecular weight is given. Error values are given except when their mathematical rounding gives 0
  4. d Theoretical radii of gyration calculated for a monomeric globular/dimeric globular/unfolded protein