The crystal structure of the EspB-EspK virulence factor-chaperone complex suggests an additional type VII secretion mechanism in M. tuberculosis.

Gijsbers A, Eymery M, Gao Y, Menart I, Vinciauskaite V, Siliqi D, Peters PJ, McCarthy A, Ravelli RBG, J Biol Chem :102761 (2022) Europe PMC

SASDQF4 – ESX-1 secretion-associated protein EspB

ESX-1 secretion-associated protein EspB
MWexperimental 318 kDa
MWexpected 261 kDa
VPorod 911 nm3
log I(s) 3.09×102 3.09×101 3.09×100 3.09×10-1
ESX-1 secretion-associated protein EspB small angle scattering data  s, nm-1
ln I(s)
ESX-1 secretion-associated protein EspB Guinier plot ln 3.10×102 Rg: 5.9 nm 0 (5.9 nm)-2 s2
(sRg)2I(s)/I(0)
ESX-1 secretion-associated protein EspB Kratky plot 1.104 0 3 sRg
p(r)
ESX-1 secretion-associated protein EspB pair distance distribution function Rg: 5.9 nm 0 Dmax: 18.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the ESX-1 secretion-associated protein EspB (medium construct) in 20 mM Tris-HCl, 300 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 6.7 mg/ml was injected at a 0.08 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 20°C. 900 successive 1 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.

ESX-1 secretion-associated protein EspB
Mol. type   Protein
Organism   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Olig. state   Heptamer
Mon. MW   37.2 kDa
 
UniProt   P9WJD9 (2-348)
Sequence   FASTA