2gp8
From Proteopedia
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| - | [[Image:2gp8.gif|left|200px]] | + | [[Image:2gp8.gif|left|200px]] |
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| - | '''NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN''' | + | {{Structure |
| + | |PDB= 2gp8 |SIZE=350|CAPTION= <scene name='initialview01'>2gp8</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GP8 is a [ | + | 2GP8 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10764583 10764583] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia phage py54]] | [[Category: Yersinia phage py54]] | ||
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[[Category: scaffolding protein]] | [[Category: scaffolding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:07:20 2008'' |
Revision as of 15:07, 20 March 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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