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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis

Jyotsna Nagpal1, Jason J Paxman1, Jessica E Zammit1

  • 1Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 3086, Australia.

Scientific Reports
|December 4, 2019
PubMed

Insights

The Mycobacterium smegmatis ClpP protease forms an unusual asymmetric ClpP1P2 complex. This structure dictates how it interacts with its ATPase, differing from typical protease assemblies.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • ClpP protease is a vital component in all life forms, generally forming a 14-subunit homo-oligomeric complex.
  • This complex typically interacts symmetrically with its cognate ATPase.

Purpose of the Study:

  • To investigate the unique structure and function of the ClpP protease complex from Mycobacterium smegmatis (Msm).
  • To elucidate the mechanism of asymmetric ATPase association in the Msm ClpP1P2 complex.

Main Methods:

  • Structural characterization of the Msm ClpP1P2 complex.
  • Functional assays to determine ATPase interaction.
  • Analysis of the ClpP1 hydrophobic pocket and C-terminal extension.

Main Results:

  • Msm ClpP protease forms an asymmetric hetero-oligomeric ClpP1P2 complex, unlike typical homo-oligomeric structures.
  • The complex associates with its ATPase exclusively through the ClpP2 ring.
  • Asymmetric docking is regulated by the ClpP1 hydrophobic pocket composition and a unique C-terminal extension in ClpP1.
  • Structural analysis revealed potential product egress sites in the inactive tetradecamer.

Conclusions:

  • The Msm ClpP1P2 complex exhibits a novel asymmetric architecture for protease-ATPase interaction.
  • The unique structural features of Msm ClpP1 control ATPase binding specificity.
  • Potential product egress pathways were identified in the Msm ClpP structure.

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