2gp8
From Proteopedia
(New page: 200px<br /><applet load="2gp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gp8" /> '''NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-B...) |
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'''NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN'''<br /> | '''NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Scaffolding proteins are required for high fidelity assembly of most high | + | 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 alpha-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. |
==About this Structure== | ==About this Structure== | ||
| - | 2GP8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http:// | + | 2GP8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GP8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Yersinia phage py54]] | [[Category: Yersinia phage py54]] | ||
[[Category: Casjens, S.]] | [[Category: Casjens, S.]] | ||
| - | [[Category: Jr., P | + | [[Category: Jr., P E.Prevelige.]] |
| - | [[Category: Krishna, N | + | [[Category: Krishna, N R.]] |
| - | [[Category: Parker, M | + | [[Category: Parker, M H.]] |
[[Category: Sun, Y.]] | [[Category: Sun, Y.]] | ||
[[Category: Weigele, P.]] | [[Category: Weigele, P.]] | ||
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[[Category: scaffolding protein]] | [[Category: scaffolding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:53 2008'' |
Revision as of 15:33, 21 February 2008
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NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN
Overview
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 alpha-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.
About this Structure
2GP8 is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus., Sun Y, Parker MH, Weigele P, Casjens S, Prevelige PE Jr, Krishna NR, J Mol Biol. 2000 Apr 14;297(5):1195-202. PMID:10764583
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