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Cryo-EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution

Andrzej Szewczak-Harris1, James Wagstaff1, Jan Löwe1

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

FEBS Letters
|June 6, 2019
PubMed

Insights

The bacterial cell division MinCDE system uses MinC and MinD proteins to position the division site. Researchers visualized the MinCD protein filament structure using cryo-electron microscopy, revealing its assembly mechanism.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • The MinCDE system is crucial for bacterial cell division, ensuring the Z-ring assembles at the mid-cell.
  • MinD binds to membranes and, with MinC, inhibits FtsZ polymerization, preventing aberrant cell division.
  • MinC and MinD form polymeric structures in solution and on membranes.

Purpose of the Study:

  • To determine the high-resolution structure of copolymeric MinCD filaments from Pseudomonas aeruginosa.
  • To elucidate the assembly mechanism of MinCD filaments on lipid membranes.

Main Methods:

  • High-resolution cryo-electron microscopy (cryo-EM) was used to visualize MinCD filaments.
  • Lipid membranes were utilized to study filament assembly in a near-native context.

Main Results:

  • The cryo-EM structure revealed that MinCD filaments consist of three protofilaments formed by alternating MinC and MinD dimers.
  • These MinCD protofilaments are nearly straight.
  • Single protofilaments of MinCD were observed to assemble on lipid membranes.

Conclusions:

  • The structure provides insights into the molecular organization of MinCD filaments.
  • Understanding the assembly of MinCD on membranes contributes to deciphering the MinCDE system's mechanism for cell division site positioning.
Keywords:
WACAbacterial cytoskeletoncell divisioncryo-EMhelical reconstructionprotein filaments

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