Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.

@article{Cha2010CrystalSO,
  title={Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.},
  author={Sun-Shin Cha and Young Jun An and Chang Ro Lee and Hyun Sook Lee and Yeon-Gil Kim and Sang Jin Kim and Kae Kyoung Kwon and Gian Marco De Donatis and Jung-Hyun Lee and Michael R. Maurizi and Sung Gyun Kang},
  journal={The EMBO journal},
  year={2010},
  volume={29 20},
  pages={3520-30}
}
Lon proteases are distributed in all kingdoms of life and are required for survival of cells under stress. Lon is a tandem fusion of an AAA+ molecular chaperone and a protease with a serine-lysine catalytic dyad. We report the 2.0-Å resolution crystal structure of Thermococcus onnurineus NA1 Lon (TonLon). The structure is a three-tiered hexagonal cylinder with a large sequestered chamber accessible through an axial channel. Conserved loops extending from the AAA+ domain combine with an… CONTINUE READING
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