2gp8
From Proteopedia
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| - | [[ | + | ==NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN== |
| + | <StructureSection load='2gp8' size='340' side='right' caption='[[2gp8]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2gp8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GP8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GP8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gp8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gp8 RCSB], [http://www.ebi.ac.uk/pdbsum/2gp8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:10764583</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Enterobacteria phage p22]] | [[Category: Enterobacteria phage p22]] | ||
| - | [[Category: Casjens, S | + | [[Category: Casjens, S]] |
| - | [[Category: Krishna, N R | + | [[Category: Krishna, N R]] |
| - | [[Category: Parker, M H | + | [[Category: Parker, M H]] |
| - | [[Category: Prevelige, P E | + | [[Category: Prevelige, P E]] |
| - | [[Category: Sun, Y | + | [[Category: Sun, Y]] |
| - | [[Category: Weigele, P | + | [[Category: Weigele, P]] |
[[Category: Coat protein-binding domain]] | [[Category: Coat protein-binding domain]] | ||
[[Category: Helix-loop-helix motif]] | [[Category: Helix-loop-helix motif]] | ||
[[Category: Scaffolding protein]] | [[Category: Scaffolding protein]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
Revision as of 06:48, 22 December 2014
NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN
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