Conformational Changes of RORĪ³ During Response Element Recognition and Coregulator Engagement

Strutzenberg T, Zhu Y, Novick S, Garcia-Ordonez R, Doebelin C, He Y, Ra Chang M, Kamenecka T, Edwards D, Griffin P, Journal of Molecular Biology :167258 (2021) DOI

SASDLE5 – RORg2 bound to a Classic-RORgamma Response Element

Retinoid-related orphan receptor-gamma
Classic-RORgamma Response Element
MWI(0) 65 kDa
MWexpected 75 kDa
VPorod 132 nm3
log I(s) 1.54×101 1.54×100 1.54×10-1 1.54×10-2
Retinoid-related orphan receptor-gamma Classic-RORgamma Response Element small angle scattering data  s, nm-1
ln I(s)
Retinoid-related orphan receptor-gamma Classic-RORgamma Response Element Guinier plot ln 1.54×101 Rg: 5.5 nm 0 (5.5 nm)-2 s2
(sRg)2I(s)/I(0)
Retinoid-related orphan receptor-gamma Classic-RORgamma Response Element Kratky plot 1.104 0 3 sRg
p(r)
Retinoid-related orphan receptor-gamma Classic-RORgamma Response Element pair distance distribution function Rg: 5.8 nm 0 Dmax: 22.9 nm

Data validation


Fits and models


log I(s)
 s, nm-1
RORg2 bound to a Classic-RORgamma Response Element Rg histogram Rg, nm

Synchrotron SAXS data from solutions of RORg2 bound to a Classic-RORgamma Response Element in 25 mM HEPES, 150 mM TCEP, 2% Glycerol, 5 mM DTT, pH 7.5 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.14 mg/ml was measured at 10°C. 33 successive 0.300 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.

Retinoid-related orphan receptor-gamma (RORg)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   55.9 kDa
 
UniProt   P51449 (25-518)
Sequence   FASTA
 
Classic-RORgamma Response Element (cRORE)
Mol. type   DNA
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   9.3 kDa
Sequence   FASTA