Sas20 is a highly flexible starch-binding protein in the Ruminococcus bromii cell-surface amylosome

Cerqueira F, Photenhauer A, Doden H, Brown A, Abdel-Hamid A, Moraïs S, Bayer E, Wawrzak Z, Cann I, Ridlon J, Hopkins J, Koropatkin N, Journal of Biological Chemistry :101896 (2022) DOI

SASDN32 – Dockerin domain-containing protein, starch adherence system 20 (Sas20), domain 2 with maltoheptaose

Dockerin domain-containing protein
MWexperimental 26 kDa
MWexpected 26 kDa
VPorod 41 nm3
log I(s) 2.52×10-2 2.52×10-3 2.52×10-4 2.52×10-5
Dockerin domain-containing protein small angle scattering data  s, nm-1
ln I(s)
Dockerin domain-containing protein Guinier plot ln 2.52×10-2 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Dockerin domain-containing protein Kratky plot 1.104 0 √3 sRg
p(r)
Dockerin domain-containing protein pair distance distribution function Rg: 2.1 nm 0 Dmax: 7.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Dockerin domain-containing protein MULTIFOXS model
Synchrotron SAXS data from solutions of Dockerin domain-containing protein, starch adherence system 20 (Sas20), domain 2 with maltoheptaose in phosphate buffered saline, 1 mM TCEP, pH 7 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.6 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 10.00 mg/ml was measured at 23°C. 2500 successive 0.700 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.

Dockerin domain-containing protein (Doc20)
Mol. type   Protein
Organism   Ruminococcus bromii
Olig. state   Monomer
Mon. MW   25.9 kDa
 
UniProt   A0A2N0URA4 (32-269)
Sequence   FASTA