Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems

Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K, (2018) DOI

SASDDV2 – EspG5 chaperone from Mycobacterium tuberculosis

EspG5 chaperone from Mycobacterium tuberculosis

MW^experimental	22	kDa
MW^expected	32	kDa

log I(s) 5.51×10² 5.51×10¹ 5.51×10⁰ 5.51×10^-1

EspG5 chaperone from Mycobacterium tuberculosis small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

EspG5 chaperone from Mycobacterium tuberculosis Guinier plot

ln 5.52×10² R_g: 2.4 nm 0 (2.4 nm)^-2 s²

(sR_g)²I(s)/I(0)

EspG5 chaperone from Mycobacterium tuberculosis Kratky plot

1.104 0 √3 sR_g

p(r)	R_g: 2.4 nm 0 D_max: 8 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.5

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.248
0.980

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

EspG5 chaperone from Mycobacterium tuberculosis Rg histogram

R_g, nm

Synchrotron SAXS data from solutions of EspG5 chaperone from Mycobacterium tuberculosis in 20 mM HEPES pH 7.5, 150 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.70 mg/ml was measured at 20°C. 20 successive 0.050 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Sample detector distance = UNKNOWN

EspG5 chaperone from Mycobacterium tuberculosis (EspG5Mtb)
Mol. type		Protein
Organism		Mycobacterium tuberculosis
Olig. state		Monomer
Mon. MW		32.4 kDa

UniProt		O53943
Sequence		FASTA