Structural insights into the mechanism of c-di-GMP-bound YcgR regulating flagellar motility in Escherichia coli.

Hou YJ, Yang WS, Hong Y, Zhang Y, Wang DC, Li DF, J Biol Chem 295(3):808-821 (2020) Europe PMC

SASDEB9 – Flagellar brake protein YcgR from Escherichia coli

Flagellar brake protein YcgR
MWexperimental 29 kDa
MWexpected 29 kDa
VPorod 44 nm3
log I(s) 2.18×103 2.18×102 2.18×101 2.18×100
Flagellar brake protein YcgR small angle scattering data  s, nm-1
ln I(s)
Flagellar brake protein YcgR Guinier plot ln 2.18×103 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Flagellar brake protein YcgR Kratky plot 1.104 0 √3 sRg
p(r)
Flagellar brake protein YcgR pair distance distribution function Rg: 2.7 nm 0 Dmax: 9.1 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Flagellar brake protein YcgR SASREF model
log I(s)
 s, nm-1
Flagellar brake protein YcgR DAMMIF model
Synchrotron SAXS data from solutions of the flagellar brake protein, YcgR in 20 mM HEPES, 150mM NaCl, 10% glycerol, pH 7.5 were collected on the BL19U2 beam line at the Shanghai Synchrotron Radiation Facility (SSRF; Shanghai, China) using a Pilatus 1M detector at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 4°C. 20 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.

Sample detector distance = UNKNOWN

Flagellar brake protein YcgR
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   29.4 kDa
 
UniProt   P76010
Sequence   FASTA