The Arthropoda-specific Tramtrack group BTB protein domains use previously unknown interface to form hexamers.

Bonchuk AN, Balagurov KI, Baradaran R, Boyko KM, Sluchanko NN, Khrustaleva AM, Burtseva AD, Arkova OV, Khalisova KK, Popov VO, Naschberger A, Georgiev PG, Elife 13 (2024) Europe PMC

SASDP59 – BTB domain of longitudinals lacking (LOLA) protein

Longitudinals lacking protein, isoform G
MWexperimental 122 kDa
MWexpected 92 kDa
VPorod 189 nm3
log I(s) 6.30×10-2 6.30×10-3 6.30×10-4 6.30×10-5
Longitudinals lacking protein, isoform G small angle scattering data  s, nm-1
ln I(s)
Longitudinals lacking protein, isoform G Guinier plot ln 6.31×10-2 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
Longitudinals lacking protein, isoform G Kratky plot 1.104 0 3 sRg
Dmax: 14.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Longitudinals lacking protein, isoform G ALPHAFOLD model

Synchrotron SAXS data from solutions of the BTB domain from LOLA protein in 20 mM Tris, pH 7.4, 200 mM NaCl, 1 mM DTT, were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 3 mg/ml were measured at 10°C. 30 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Longitudinals lacking protein, isoform G (LOLA)
Mol. type   Protein
Organism   Drosophila melanogaster
Olig. state   Hexamer
Mon. MW   15.3 kDa
 
UniProt   P42283 (1-120)
Sequence   FASTA