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Related Experiment Videos

Thermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.

K S Makarova1, N V Grishin

  • 1National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894, USA.

Protein Science : a Publication of the Protein Society
|December 14, 1999
PubMed
Summary

Two distinct zinc-dependent proteases, thermolysin and mitochondrial processing peptidase (MPP), exhibit remarkable structural and functional convergence. This suggests limited evolutionary pathways for creating effective zinc-protease enzymes.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Thermolysin and mitochondrial processing peptidase (MPP) are Zn-dependent proteases.
  • These enzymes, though nonhomologous, share functional similarities with other proteases like chymotrypsin and subtilisin.

Purpose of the Study:

  • To describe the structure-functional convergence between thermolysin and MPP.
  • To understand the evolutionary constraints in zinc-protease active site and architecture.

Main Methods:

  • Comparative structural analysis of thermolysin and MPP.
  • Analysis of active site residue conservation and arrangement.
  • Examination of overall molecular architecture, including beta-sheet and alpha-helix packing.

Main Results:

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  • Identified functional convergence in active site residues and structural convergence in overall molecular architecture between thermolysin and MPP.
  • Observed similar beta-sheet arrangements and alpha-helix packing despite different topological connections and main-chain orientations.
  • Rationalized the sequence "inversion" of the HEXXH motif in thermolysin to HXXEH in MPP.

Conclusions:

  • The convergence suggests limited evolutionary options for constructing functional Zn-proteases.
  • Hydrogen bonding between substrate and enzyme beta-sheet is a key feature for substrate binding in these enzymes.