2GP8

NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN

2GP8 の概要

• エントリーDOI: 10.2210/pdb2gp8/pdb
• 分子名称: PROTEIN (SCAFFOLDING PROTEIN) (1 entity in total)
• 機能のキーワード: scaffolding protein, coat protein-binding domain, helix-loop-helix motif, viral protein
• 由来する生物種: Enterobacteria phage P22
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4329.03

構造登録者

Sun, Y.,Parker, M.H.,Weigele, P.,Casjens, S.,Prevelige Jr., P.E.,Krishna, N.R. (登録日: 1999-05-11, 公開日: 1999-05-17, 最終更新日: 2023-12-27)

主引用文献

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

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: 10764583
DOI: 10.1006/jmbi.2000.3620

実験手法

SOLUTION NMR