Structural and biophysical characterization of the proteins interacting with the herpes simplex virus 1 origin of replication.

Manolaridis I, Mumtsidu E, Konarev P, Makhov AM, Fullerton SW, Sinz A, Kalkhof S, McGeehan JE, Cary PD, Griffith JD, Svergun D, Kneale GG, Tucker PA, J Biol Chem 284(24):16343-16353 (2009) Europe PMC

SASDLU5 – Complex formed between the replication origin-binding protein UL9 (C-terminal domains) with 15-bp DNA

Replication origin-binding protein
15-bp DNA
MWI(0) 81 kDa
MWexpected 90 kDa
log I(s) 7.19×101 7.19×100 7.19×10-1 7.19×10-2
Replication origin-binding protein 15-bp DNA small angle scattering data  s, nm-1
ln I(s)
Replication origin-binding protein 15-bp DNA Guinier plot ln 7.19×101 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Replication origin-binding protein 15-bp DNA Kratky plot 1.104 0 √3 sRg
Dmax: 15 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Replication origin-binding protein 15-bp DNA MONSA model
Synchrotron SAXS data from solutions of the complex between UL9ct protein and 15-bp DNA in 20 mM Tris-HCl, 50 mM NaCl, 5 mM MgCl2, pH 7.5 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 15°C. One 120 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Tags: X33
Replication origin-binding protein (UL9)
Mol. type   Protein
Organism   Human herpesvirus 1 (strain 17)
Olig. state   Dimer
Mon. MW   40.6 kDa
 
UniProt   P10193 (487-851)
Sequence   FASTA
 
15-bp DNA (15-bp DNA)
Mol. type   DNA
Olig. state   Monomer
Mon. MW   9.3 kDa
Sequence   FASTA