The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.

Tarbouriech N, Ducournau C, Hutin S, Mas PJ, Man P, Forest E, Hart DJ, Peyrefitte CN, Burmeister WP, Iseni F, Nat Commun 8(1):1455 (2017) Europe PMC

SASDCN5 – Vaccinia virus DNA polymerase

DNA polymerase E9
MWexperimental 117 kDa
MWexpected 117 kDa
VPorod 202 nm3
log I(s) 1.99×101 1.99×100 1.99×10-1 1.99×10-2
DNA polymerase E9 small angle scattering data  s, nm-1
ln I(s)
DNA polymerase E9 Guinier plot ln 2.00×101 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
DNA polymerase E9 Kratky plot 1.104 0 √3 sRg
p(r)
DNA polymerase E9 pair distance distribution function Rg: 3.6 nm 0 Dmax: 12 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DNA polymerase E9 PYMOL model
Synchrotron SAXS data from solutions of Vaccinia virus DNA polymerase in 20 mM Tris HCl, 100 mM NaCl, 4 mM DTT, pH 7 using size exclusion chromatography coupled SAXS (SEC-SAXS) 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 = 0.0992 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Data were collected at at 20°C during the course of elution (900 successive 1 second frames). The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the resulting subtracted curves were scaled and averaged.

Concentration min = UNKNOWN. Concentration max = UNKNOWN

DNA polymerase E9 (E9)
Mol. type   Protein
Organism   Vaccinia virus
Olig. state   Monomer
Mon. MW   117.2 kDa
 
UniProt   P20509 (1-1006)
Sequence   FASTA
 
PDB ID   5N2E