Conformational plasticity of the essential membrane-associated mannosyltransferase PimA from mycobacteria.

Giganti D, Alegre-Cebollada J, Urresti S, Albesa-Jové D, Rodrigo-Unzueta A, Comino N, Kachala M, López-Fernández S, Svergun DI, Fernández JM, Guerin ME, J Biol Chem 288(41):29797-808 (2013) Europe PMC

SASDAS4 – I27-PimA

I27-PimA Fusion protein
MWexperimental 45 kDa
MWexpected 48 kDa
VPorod 86 nm3
log I(s) 4.34×101 4.34×100 4.34×10-1 4.34×10-2
I27-PimA Fusion protein small angle scattering data  s, nm-1
ln I(s)
I27-PimA Fusion protein Guinier plot ln 4.34×101 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
I27-PimA Fusion protein Kratky plot 1.104 0 √3 sRg
p(r)
I27-PimA Fusion protein pair distance distribution function 0 Dmax: 10.7 nm

Data validation

Fits and models

log I(s)
 s, nm-1
I27-PimA Fusion protein MONSA model
log I(s)
 s, nm-1
I27-PimA Fusion protein MONSA model
Synchrotron SAXS data from solutions of I27-PimA in 50 mM Tris-HCl 150 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.4 and 2.5 mg/ml were measured at 10°C. 50 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.

I27-PimA Fusion protein (I27-PimA)
Mol. type   Protein
Olig. state   Monomer
Mon. MW   48.4 kDa