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Related Experiment Video

Updated: May 17, 2026

Investigation of Microbial Cooperation via Imaging Mass Spectrometry Analysis of Bacterial Colonies Grown on Agar and in Tissue During Infection
09:49

Investigation of Microbial Cooperation via Imaging Mass Spectrometry Analysis of Bacterial Colonies Grown on Agar and in Tissue During Infection

Published on: November 18, 2022

Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment.

Alison C Pitts1, Laura R Tuck, Alexandra Faulds-Pain

  • 1Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.

Plos One
|November 13, 2012
PubMed
Summary
This summary is machine-generated.

Clostridium difficile forms bacterial microcompartments using the eut operon for ethanolamine metabolism. Structural analysis reveals shell protein organization crucial for microcompartment assembly and function in this pathogen.

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Culturing and Maintaining Clostridium difficile in an Anaerobic Environment
11:13

Culturing and Maintaining Clostridium difficile in an Anaerobic Environment

Published on: September 14, 2013

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Last Updated: May 17, 2026

Investigation of Microbial Cooperation via Imaging Mass Spectrometry Analysis of Bacterial Colonies Grown on Agar and in Tissue During Infection
09:49

Investigation of Microbial Cooperation via Imaging Mass Spectrometry Analysis of Bacterial Colonies Grown on Agar and in Tissue During Infection

Published on: November 18, 2022

Culturing and Maintaining Clostridium difficile in an Anaerobic Environment
11:13

Culturing and Maintaining Clostridium difficile in an Anaerobic Environment

Published on: September 14, 2013

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Bacterial microcompartments (BMCs) are protein shells protecting enzymes processing unstable intermediates.
  • Clostridium difficile, a virulent pathogen, possesses a eut operon for ethanolamine metabolism.
  • Homologous BMC loci exist in other enteric pathogens like Salmonella and Enterococcus.

Purpose of the Study:

  • To determine the crystal structures of key proteins involved in the C. difficile eut microcompartment.
  • To investigate the self-assembly properties of microcompartment shell proteins.
  • To provide a structural basis for understanding BMC architecture and function in C. difficile.

Main Methods:

  • X-ray crystallography was used to determine the structures of CD1908, CD1918, and CD1925.
  • Thin-section transmission electron microscopy (TEM) was employed to visualize protein assembly.
  • Bioinformatic analysis of homologous loci in other bacterial genomes.

Main Results:

  • CD1908 and CD1918 share a common protein fold, forming hexamers with structural variations.
  • CD1925 exhibits a cupin β-barrel fold with a unique putative active site.
  • TEM revealed CD1918 self-associates into arrays, indicating a role in microcompartment organization.

Conclusions:

  • The structural data elucidate the building blocks of the C. difficile eut microcompartment.
  • CD1918's self-assembly suggests its importance in shell formation.
  • This study lays groundwork for exploring the microcompartment's metabolic role and contribution to C. difficile virulence.