Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima

Drexler D, Müller M, Rojas-Cordova C, Bandera A, Witte G, Structure 2017 Oct DOI

SASDCD7 – Thermotoga maritima phosphodiesterase TM1595 (wildtype, TmPde)

Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595)
MWexperimental 67 kDa
MWexpected 76 kDa
VPorod 105.9 nm3
log I(s) 1.97×104 1.97×103 1.97×102 1.97×101
Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) small angle scattering data  s, nm-1
ln I(s)
Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) Guinier plot ln 1.98×104 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) Kratky plot 1.104 0 3 sRg
p(r)
Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) pair distance distribution function Rg: 2.7 nm 0 Dmax: 7.8 nm

Experimental data validation


Fits and models


log I(s)
 s, nm-1
Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) PDB model
Synchrotron SAXS data from solutions of Thermotoga maritima phosphodiesterase TM1595 (wildtype, TmPde) in 20mM Tris, 200 mM NaCl, 5%(v/v) glycerol, pH 7.5, were collected on the EMBL-P12 beam line on the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.123987 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). One solute concentration of 7.00 mg/ml was measured at 20°C. 34 successive 0.045 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 and the different curves were scaled for protein concentration.

Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) (TmPde)
Mol. type   Protein
Organism   Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Olig. state   Dimer
Mon. MW   37.8 kDa
 
UniProt   Q9X1T1
Sequence   FASTA
 
PDB code   5O25