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

SASDMF7 – ESX-1 secretion-associated protein EspB small construct

ESX-1 secretion-associated protein EspB
MWexperimental 36 kDa
MWexpected 30 kDa
VPorod 56 nm3
log I(s) 4.13×10-2 4.13×10-3 4.13×10-4 4.13×10-5
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 4.13×10-2 Rg: 3.3 nm 0 (3.3 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: 3.3 nm 0 Dmax: 10.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the ESX-1 secretion-associated protein EspB (small 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 2M 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 45.00 μl sample at 5.6 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.

The sample consists of EspB spanning amino acids 7–278. The SEC-eluted protein was directed through a 1.6-mm diameter quartz capillary cell held in vacuum.

ESX-1 secretion-associated protein EspB (EspBS(7-278))
Mol. type   Protein
Organism   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Olig. state   Monomer
Mon. MW   30.1 kDa
 
UniProt   P9WJD9 (7-278)
Sequence   FASTA