Molecular comparison of Neanderthal and Modern Human adenylosuccinate lyase.

Van Laer B, Kapp U, Soler-Lopez M, Moczulska K, Pääbo S, Leonard G, Mueller-Dieckmann C, Sci Rep 8(1):18008 (2018) Europe PMC

SASDEN5 – AMP/fumarate-bound neanderthal adenylosuccinate lyase (ADSL)

Adenylosuccinate lyase

MW^experimental	168	kDa
MW^expected	221	kDa
V^Porod	258	nm³

log I(s) 1.52×10² 1.52×10¹ 1.52×10⁰ 1.52×10^-1

Adenylosuccinate lyase small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 1.53×10² R_g: 3.7 nm 0 (3.7 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

Data validation

Fits and models

log I(s)

s, nm^-1

Adenylosuccinate lyase PDB (PROTEIN DATA BANK) model

Synchrotron SAXS data from solutions of AMP/fumarate-bound neanderthal adenylosuccinate lyase (ADSL) in 10 mM HEPES, 100 mM NaCl, 1 mM DTT, 1mM AMP, 1 mM Fumarate, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Dectris Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. 10 successive 1 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.

Adenylosuccinate lyase (ADSL)
Mol. type		Protein
Organism		Homo sapiens neanderthalensis
Olig. state		Tetramer
Mon. MW		55.1 kDa

UniProt		A0A384E0N4 (1-487)
Sequence		FASTA

PDB ID		5NXA