Insights into herpesvirus assembly from the structure of the pUL7:pUL51 complex.

Butt BG, Owen DJ, Jeffries CM, Ivanova L, Hill CH, Houghton JW, Ahmed MF, Antrobus R, Svergun DI, Welch JJ, Crump CM, Graham SC, Elife 9 (2020) Europe PMC

SASDG37 – 1:2 heterotrimer of pUL7 and pUL51(8-142) from herpes simplex virus 1

Tegument protein UL7
Tegument protein UL51
MWexperimental 67 kDa
MWexpected 64 kDa
VPorod 116 nm3
log I(s) 3.33×103 3.33×102 3.33×101 3.33×100
Tegument protein UL7 Tegument protein UL51 small angle scattering data  s, nm-1
ln I(s)
Tegument protein UL7 Tegument protein UL51 Guinier plot ln 3.33×103 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
Tegument protein UL7 Tegument protein UL51 Kratky plot 1.104 0 3 sRg
p(r)
Tegument protein UL7 Tegument protein UL51 pair distance distribution function Rg: 3.0 nm 0 Dmax: 11.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Tegument protein UL7 Tegument protein UL51 DAMMIN model

log I(s)
 s, nm-1
Tegument protein UL7 Tegument protein UL51 GASBOR model

log I(s)
 s, nm-1
Tegument protein UL7 Tegument protein UL51 CORAL model

Synchrotron SAXS data from the 1:2 heterotrimer of pUL7 and pUL51(8-142) from herpes simplex virus 1 in 20 mM tris, 200 mM NaCl, 3% (v/v) glycerol, 0.25 mM TCEP, pH 7.5 were collected on the EMBL P12 beam line at PETRA III (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The profile displayed represents the average of three individual SEC-SAXS runs. The SEC parameters, per run, were as follows: A 75.00 μl sample at 4.5 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. Approximately 100 successive 1 second frames were collected through the major SEC-elution peak and processed using CHROMIXS. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

The quoted experimental molecular mass, that corresponds to a 1:2 pUL7:pUL51(8-142) heterotrimer, was determined from SEC-MALLS-RI measurements performed on identical samples, eluted in parallel to the SEC-SAXS. The SEC-SAXS data for each individual run, Rg correlations through the main elution peak as well as the the SEC-MALLS-RI data and hydrodynamic estimates obtained from QELS are made available in the full-entry zip archive. The CORAL rigid-body refined (atomistic) model displayed in this entry is one example of several alternatives whereby a second copy of pUL51 samples different spatial positions bound within the complex. Additional representations of the 1:2 pUL7:pUL51(8-142) heterotrimeric complex, including those incorporating mass spectrometry cross-linking distance constraints, are also made available in the full entry zip-archive.

Tegument protein UL7 (pUL7)
Mol. type   Protein
Organism   Human alphaherpesvirus 1 strain KOS
Olig. state   Monomer
Mon. MW   33.9 kDa
 
UniProt   A0A110B4Q7 (1-296)
Sequence   FASTA
 
Tegument protein UL51 (pUL51)
Mol. type   Protein
Organism   Human alphaherpesvirus 1 strain KOS
Olig. state   Dimer
Mon. MW   14.8 kDa
 
UniProt   D3YPL0 (8-142)
Sequence   FASTA
 
PDB code   6T5A