Functional role of the N-terminal region of the Lon protease from Mycobacterium smegmatis.

@article{Roudiak1998FunctionalRO,
  title={Functional role of the N-terminal region of the Lon protease from Mycobacterium smegmatis.},
  author={S G Roudiak and Thomas E. Shrader},
  journal={Biochemistry},
  year={1998},
  volume={37 32},
  pages={
          11255-63
        }
}
Lon protease homologues contain a poorly conserved N-terminal region of variable length. To better understand the role of the N-terminal region of Lon in the complicated reaction cycle of ATP-dependent protein degradation, we expressed and characterized mutants of the Lon protease from Mycobacterium smegmatis (Ms-Lon) lacking 90, 225, and 277 N-terminal residues (N-G91, N-E226, and N-I278, respectively). N-I278 displayed neither peptidase nor ATPase activity despite the fact that it was stable… 

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TLDR
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TLDR
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TLDR
The hypothesis that there is a structural and functional relationship between two coiled–coil fragments and implies a similar mechanism of engagement of the pore‐1 loops in the AAA+ modules of LonAs and ClpBs is supported.

Crystal structure of the N‐terminal domain of E. coli Lon protease

TLDR
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