Invariant BECN1 CXXC motifs bind Zn(2+) and regulate structure and function of the BECN1 intrinsically disordered region.

Mukhopadhyay S, Subedi S, Hopkins JB, Ugrinov A, Chakravarthy S, Colbert CL, Sinha SC, Autophagy :1-17 (2023) Europe PMC

SASDQZ9 – Beclin-1 amino acids 1-150 with two cysteine motifs, along with a C-terminal tyrosine analysed using EFA in BIOXTAS RAW software, component 0

Beclin-1
MWI(0) 34 kDa
MWexpected 17 kDa
VPorod 87 nm3
log I(s) 5.21×10-1 5.21×10-2 5.21×10-3 5.21×10-4
Beclin-1 small angle scattering data  s, nm-1
ln I(s)
Beclin-1 Guinier plot ln 5.22×10-1 Rg: 4.3 nm 0 (4.3 nm)-2 s2
(sRg)2I(s)/I(0)
Beclin-1 Kratky plot 1.104 0 √3 sRg
p(r)
Beclin-1 pair distance distribution function Rg: 4.6 nm 0 Dmax: 20 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Beclin-1 amino acids 1-150 with two cysteine motifs, analysed using evolving factor analysis (EFA, component 0), in 50 mM Tris, 300 mM NaCl, pH 8 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 22°C. 253 successive 0.500 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.

Beclin-1 (BECN1(1-150)Y)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   17.2 kDa
 
UniProt   Q14457 (1-150)
Sequence   FASTA