DegP protease

The DegP Protease Chaperone A Molecular Cage with Bouncers 275... 

The protease conformation of DegP is still elusive as crystallization of a substratelike inhibitor complex has failed and maintenance of a stably folded protein precludes long-term experimentation at elevated temperatures where it displays protease activity. We propose a profound rearrangement of the LA -L1-L2 loop triad into the canonical conformation of active serine proteases competent for substrate binding. This may be initiated by a collapse of the hydrophobic LA platforms and an enlargement of the hydrophobic contacts caused at high temperature. 

Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M., and Clausen, T. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 2002, 416, 455-459. 

Misra, R., Castillokeller, M., and Deng, M. Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background. J. Bacteriol. 2000,... 

Itzhaki H, Naveh L, Lindahl M et al. Identification and characterizsuion of DegP, a serine protease associated with the lumenal side of the thylakoid membrane. J Biol Chem 1998 273 7094—7098. 

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