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

SASDG47 – 2:4 heterohexamer of pUL7 and pUL51 from herpes simplex virus 1

Tegument protein UL7
Tegument protein UL51
MWexperimental 168 kDa
MWexpected 170 kDa
VPorod 340 nm3
log I(s) 3.10×103 3.10×102 3.10×101 3.10×100
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 3.10×103 Rg: 4.6 nm 0 (4.6 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: 4.8 nm 0 Dmax: 19.7 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

Synchrotron SAXS data from the 2:4 heterohexamer of pUL7 and pUL51 from herpes simplex virus 1 in 20 mM HEPES, 200 mM NaCl, 3% (v/v) glycerol, 1 mM DTT, 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 SEC parameters were as follows: A 90.00 μl sample at 8 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20.2°C. 48 successive 0.995 second frames were collected through the minor SEC-elution peak (corresponding to the heterohexamer) 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 2:4 pUL7:pUL51 heterohexamer, was determined from SEC-MALLS-RI measurements performed in parallel to the SEC-SAXS. The SEC-SAXS data, Rg correlations through the dimer elution peak as well as the the SEC-MALLS-RI data are made available in the full-entry zip archive. The GASBORMX model displayed in this entry represents a 100 % volume fraction of the heterohexamer in solution that has been separated from a 1:2 pUL7:pUL51 heterotrimer (refer to SASBDB entry SASDG57).

Tegument protein UL7 (pUL7)
Mol. type   Protein
Organism   Human alphaherpesvirus 1 strain KOS
Olig. state   Dimer
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   Tetramer
Mon. MW   25.4 kDa
 
UniProt   D3YPL0 (1-244)
Sequence   FASTA