Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate.

Zhang J, Gonzalez LE, Hall TMT, Nucleic Acids Res 45(5):2829-2837 (2017) Europe PMC

SASDBG6 – Ribosome biogenesis protein 15 (Nop15)

Ribosome biogenesis protein 15

MW^experimental	16	kDa
MW^expected	17	kDa
V^Porod	38	nm³

log I(s) 1.13×10² 1.13×10¹ 1.13×10⁰ 1.13×10^-1

Ribosome biogenesis protein 15 small angle scattering data

s, nm^-1

ln I(s)

Ribosome biogenesis protein 15 Guinier plot

ln 1.14×10² R_g: 2.4 nm 0 (2.4 nm)^-2 s²

(sR_g)²I(s)/I(0)

Ribosome biogenesis protein 15 Kratky plot

1.104 0 √3 sR_g

p(r)	R_g: 2.9 nm 0 D_max: 10.3 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

1.2

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.538
0.456

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Ribosome biogenesis protein 15 EOM/RANCH model

Synchrotron SAXS data from solutions of ribosome biogenesis protein 15 (Nop15) in 25 mM HEPES, 500 mM NaCl, 2 mM DTT, pH 7.5 were collected on the BL 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS, Berkeley, CA, USA) using a MAR Image Plate detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4π sin θ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.7 and 3 mg/ml were measured at 4 °C (the data displayed in this entry: 0.7 mg/ml). One 0.5 second frame was collected per sample. The data were normalized to the intensity of the transmitted beam, radially averaged and the scattering of the solvent-blank was subtracted.

Ribosome biogenesis protein 15 (Nop15)
Mol. type		Protein
Organism		Saccharomyces cerevisiae
Olig. state		Monomer
Mon. MW		16.5 kDa

UniProt		P53927 (81-220)
Sequence		FASTA

PDB code		5T9P