Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein.

Shin J, Singal B, Manimekalai MSS, Chen MW, Ragunathan P, Grüber G, FEBS J (2020) Europe PMC

SASDHJ8 – ACT domain of the Mycobacterium tuberculosis Rel protein

ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA)
MWexperimental 18 kDa
MWexpected 20 kDa
VPorod 29 nm3
log I(s) 3.76×101 3.76×100 3.76×10-1 3.76×10-2
ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) small angle scattering data  s, nm-1
ln I(s)
ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) Guinier plot ln 3.77×101 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) Kratky plot 1.104 0 3 sRg
p(r)
ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) pair distance distribution function Rg: 1.9 nm 0 Dmax: 6.1 nm

Data validation


There are no models related to this curve.

SAXS data from solutions of the ACT domain of the M. tuberculosis Rel protein in 50 mM Tris-HCl, 350 mM NaCl, 5% glycerol, 1 mM DTT, pH 8.5 were collected using a Bruker NanoStar instrument at Nanyang Technological University (Singapore) equipped with a VÅNTEC 2000 detector at a sample-detector distance of 0.7 m and at a wavelength of λ = 0.134 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.30 mg/ml was measured at 15°C. Six successive 300 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.

ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) (MtRel ACT)
Mol. type   Protein
Organism   Mycobacterium tuberculosis
Olig. state   Dimer
Mon. MW   10.1 kDa
 
UniProt   P9WHG9 (660-738)
Sequence   FASTA