Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus 1 1 Edited by M. Summers

Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded... Scaffolding proteins are required for high fidelity assembly of most high T number dsDNA viruses such as the large bacteriophages, and the herpesvirus family. They function by transiently binding and positioning the coat protein subunits during capsid assembly. In both bacteriophage P22 and the herpesviruses the extreme scaffold C terminus is highly charged, is predicted to be an amphipathic α-helix, and is sufficient to bind the coat protein, suggesting a common mode of action. NMR studies show that the coat protein-binding domain of P22 scaffolding protein exhibits a helix-loop-helix motif stabilized by a hydrophobic core. One face of the motif is characterized by a high density of positive charges that could interact with the coat protein through electrostatic interactions. Results from previous studies with a truncation fragment and the observed salt sensitivity of the assembly process are explained by the NMR structure. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Molecular Biology Elsevier

Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus 1 1 Edited by M. Summers

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Publisher
Elsevier
Copyright
Copyright © 2000 Academic Press
ISSN
0022-2836
DOI
10.1006/jmbi.2000.3620
Publisher site
See Article on Publisher Site

Abstract

Scaffolding proteins are required for high fidelity assembly of most high T number dsDNA viruses such as the large bacteriophages, and the herpesvirus family. They function by transiently binding and positioning the coat protein subunits during capsid assembly. In both bacteriophage P22 and the herpesviruses the extreme scaffold C terminus is highly charged, is predicted to be an amphipathic α-helix, and is sufficient to bind the coat protein, suggesting a common mode of action. NMR studies show that the coat protein-binding domain of P22 scaffolding protein exhibits a helix-loop-helix motif stabilized by a hydrophobic core. One face of the motif is characterized by a high density of positive charges that could interact with the coat protein through electrostatic interactions. Results from previous studies with a truncation fragment and the observed salt sensitivity of the assembly process are explained by the NMR structure.

Journal

Journal of Molecular BiologyElsevier

Published: Apr 14, 2000

References

  • The structure of tetratricopeptide repeats of protein phosphatase
    Das, A.K.; Cohen, P.W.A.; Burford, D.
  • Classical electrostatics in biology and chemistry
    Honig, B.; Nicholls, A.
  • Bacteriophage P22 scaffolding protein forms oligomers in solution
    Parker, M.H.; Stafford, W.F.; Prevelige, P.
  • Cloning, purification, and preliminary characterization by circular dichroism and NMR of a carboxyl-terminal domain of the bacteriophage P22 scaffolding protein
    Parker, M.H.; Jablonsky, M.; Casjens, S.; Sampson, L.; Krishna, N.R.; Prevelige, P.E.
  • Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy
    Thuman-Commike, P.A.; Greene, B.; Jakana, J.; Prasad, B.V.; King, J.; Prevelige, P.E.; Chiu, W.
  • A helical coat protein recognition domain of the bacteriophage P22 scaffolding protein
    Tuma, R.; Parker, M.H.; Weigele, P.; Sampson, L.; Sun, Y.; Krishna, N.R.; Casjens, S.; Thomas, G.J.; Prevelige, P.E.

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