Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme.

Bezem MT, Baumann A, Skjærven L, Meyer R, Kursula P, Martinez A, Flydal MI, Sci Rep 6:30390 (2016) Europe PMC

SASDBZ4 – Tyrosine hydroxylase (Isoform 1, Homo sapiens)

Tyrosine hydroxylase, isoform 1

MW^experimental	284	kDa
MW^expected	222	kDa
V^Porod	520	nm³

log I(s) 6.24×10⁴ 6.24×10³ 6.24×10² 6.24×10¹

Tyrosine hydroxylase, isoform 1 small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

Tyrosine hydroxylase, isoform 1 Guinier plot

ln 6.25×10⁴ R_g: 4.7 nm 0 (4.7 nm)^-2 s²

(sR_g)²I(s)/I(0)

Tyrosine hydroxylase, isoform 1 Kratky plot

1.104 0 √3 sR_g

p(r)	R_g: 4.9 nm 0 D_max: 20 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.8

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.002
0.514

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Tyrosine hydroxylase, isoform 1 BUNCH model

X-ray synchrotron radiation scattering data from solutions of tyrosine hydroxylase, isoform 1 in 20 mM Na-HEPES, 200 mM NaCl, pH 7.0 were collected on the P12 beam line of Petra-III (Hamburg, Germany) using a Pilatus 2M detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.124 nm). Different solute concentrations in the range 1.0-2.0 mg/ml were measured using an exposure time of 1 s (recorded as 20 x 0.050 s frames). The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering from the matched solvent-blank was subtracted. The data presented here are merged SAXS data derived from the solute concentration series.

Tyrosine hydroxylase, isoform 1 (TYH)
Mol. type		Protein
Organism		Homo sapiens
Olig. state		Tetramer
Mon. MW		55.6 kDa

UniProt		P07101 (1-497)
Sequence		FASTA

PDB ID		1TOH

PDB ID		2MDA