The C-terminal tail of the bacterial translocation ATPase SecA modulates its activity.

Jamshad M, Knowles TJ, White SA, Ward DG, Mohammed F, Rahman KF, Wynne M, Hughes GW, Kramer G, Bukau B, Huber D, Elife 8 (2019) Europe PMC

SASDDY9 – Protein translocase subunit SecA (full length, amino acids 1-901)

Protein translocase subunit SecA
MWI(0) 225 kDa
MWexpected 204 kDa
VPorod 424 nm3
log I(s) 1.44×102 1.44×101 1.44×100 1.44×10-1
Protein translocase subunit SecA small angle scattering data  s, nm-1
ln I(s)
Protein translocase subunit SecA Guinier plot ln 1.44×102 Rg: 4.2 nm 0 (4.2 nm)-2 s2
Protein translocase subunit SecA Kratky plot 1.104 0 3 sRg
Protein translocase subunit SecA pair distance distribution function Rg: 4.2 nm 0 Dmax: 14.9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data, I(s) vs s (s = 4π sin θ/λ, where 2θ is the scattering angle) were collected from a sample of full length SecA using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France). Data were collected using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.0919 nm. The SEC mobile phase consisted of 20mM HEPES, 100mM NaCl, 1mM TCEP, pH 8 (20°C). Data obtained from solute-free eluates and SEC-elution peak (45 successive 1 s data frames) were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted from the SEC-peak frames to produce the data displayed in this entry.

Additional SEC parameters: Column type, S200 10/300 GL (GE Lifesciences); Flow rate, 1.0mL/min; Sample injection concentration, 5mg/mL; Injection volume, 0.5mL

Protein translocase subunit SecA
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   102.0 kDa
UniProt   P10408
Sequence   FASTA