Structure-function analyses reveal Arabidopsis thaliana HDA7 to be an inactive histone deacetylase

Saharan K, Baral S, Shaikh N, Vasudevan D, Current Research in Structural Biology :100136 (2024) DOI

SASDUK2 – Histone deacetylase 7

Histone deacetylase 7
MWexperimental 44 kDa
MWexpected 44 kDa
VPorod 85 nm3
log I(s) 6.81×101 6.81×100 6.81×10-1 6.81×10-2
Histone deacetylase 7 small angle scattering data  s, nm-1
ln I(s)
Histone deacetylase 7 Guinier plot ln 6.82×101 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Histone deacetylase 7 Kratky plot 1.104 0 √3 sRg
p(r)
Histone deacetylase 7 pair distance distribution function Rg: 3.0 nm 0 Dmax: 10.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Histone deacetylase 7 COOT model
Synchrotron SAXS data from solutions of histone deacetylase 7 in 20 mM Tris, 150 mM NaCl, 1 mM β-mercaptoethanol, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09794 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 20°C. 10 successive 5 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.

Possibly aggregated.

Histone deacetylase 7
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Monomer
Mon. MW   43.9 kDa
 
UniProt   Q9FH09 (5-383)
Sequence   FASTA