Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.

@article{Rizzo2014MultipleFR,
  title={Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.},
  author={Alessandro A. Rizzo and Margaret M Suhanovsky and Matthew L. Baker and LaTasha C R Fraser and Lisa M. Jones and Don L. Rempel and Michael L Gross and Wah Chiu and Andrei T. Alexandrescu and Carolyn M Teschke},
  journal={Structure},
  year={2014},
  volume={22 6},
  pages={830-41}
}
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique insertion domain (I-domain). Two prior I-domain models from subnanometer cryoelectron microscopy (cryoEM) reconstructions differed substantially. Therefore, the I-domain's nuclear magnetic resonance structure was determined and also used to improve cryoEM models of coat protein. The I-domain has an antiparallel six-stranded β-barrel fold, not… CONTINUE READING
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