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Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416 , 455 (2002) Speaker : Tsai, Jia-Yin. Outline. Functions of molecular chaperones and protease The properties of DegP (HtrA) family The relationship between HP1019 and DegP The crystal structure of DegP.

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Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

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  1. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine Nature 416, 455 (2002) Speaker : Tsai, Jia-Yin

  2. Outline • Functions of molecular chaperones and protease • The properties of DegP (HtrA) family • The relationship between HP1019 and DegP • The crystal structure of DegP

  3. Functions of molecular chaperones and protease • When Is Quality Control Necessary? • Protein triage model for quality control Science286, 73 (1999)

  4. The families of chaperones • The Hsp60 or GroEL family (chaperonines) • The Hsp70 or DnaK family • The Cip or Hsp100 family

  5. The families of proteases Science286, 73 (1999)

  6. Cell91, 435 (1997)

  7. Science286, 73 (1999)

  8. The DegP (HtrA) family • HtrA (High-temperature requirement A), also known as DegP and probably identical to the Do protease, is a heat shock-induced serine protease that is located in the periplasmic space of Escherichia coli. • Mature DegP has 448 residues of which His-105, Asp-135, and Ser-210 are postulated to be the catalytic triad residues.

  9. PDZ PDZ PDZ HhoA (DegQ) PDZ PDZ PDZ IGFB K PDZ PDZ PDZ HtrA (DegP) H D S H D S H D S H D S H D S HhoB (DegS) L56 (human) S PDZ N1897 Primary structure of HtrA and related proteins Mol. Microbiol.26, 209 (1997)

  10. Functionsof PDZ domain • The PDZ domain is named after three of the proteins in which the repeats have been described: PSD-95, Dig and Zo-1 • Modular PDZ domains, found in many cell junction–associated proteins, mediate the clustering of membrane ion channels by binding to their C-terminus.

  11. Three-Dimensional Fold of the PDZ-3 Domain from PSD-95 Cell85, 1067 (1996)

  12. HP1091 (HtrA) Protein

  13. DegP HP1091

  14. The sequences alignment between HP1019 and DegP(S210A)

  15. Materials and Methods • The used a proteolytically inactive mutant for structural determination (S210A). • The mutant S210A was crystallized at 180C. After successful crystallization, the crystal was transferred to 40C, by locking the protein in “chaperone conformation”.

  16. Protease Protease PDZ2 PDZ2 PDZ1 PDZ1 Structure of DegP

  17. Peptide-binding sites of PDZ1 and PDZ2

  18. The protease domain

  19. The central cavity

  20. Thank You!!!

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