1GP8
NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN
Summary for 1GP8
| Entry DOI | 10.2210/pdb1gp8/pdb |
| Descriptor | PROTEIN (SCAFFOLDING PROTEIN) (1 entity in total) |
| Functional Keywords | scaffolding protein, coat protein-binding domain, helix-loop-helix motif, viral protein |
| Biological source | Enterobacteria phage P22 |
| Total number of polymer chains | 1 |
| Total formula weight | 4329.03 |
| Authors | Sun, Y.,Parker, M.H.,Weigele, P.,Casjens, S.,Prevelige Jr., P.E.,Krishna, N.R. (deposition date: 1999-05-11, release date: 1999-05-17, Last modification date: 2023-12-27) |
| Primary citation | Sun, Y.,Parker, M.H.,Weigele, P.,Casjens, S.,Prevelige Jr., P.E.,Krishna, N.R. Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus. J.Mol.Biol., 297:1195-1202, 2000 Cited by PubMed 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 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. PubMed: 10764583DOI: 10.1006/jmbi.2000.3620 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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