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Related Experiment Video

Updated: Apr 30, 2026

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
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Gas-phase structure of the E. coli OmpA dimer.

Julian Whitelegge1

  • 1Pasarow Mass Spectrometry Laboratory, NPI-Semel Institute, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.

Structure (London, England : 1993)
|May 9, 2014
PubMed
Summary

Gas-phase collisional cross section (CCS) analysis of E. coli outer membrane OmpA oligomers reveals structural insights. The dimer

Area of Science:

  • Structural biology
  • Biophysics
  • Mass spectrometry

Background:

  • The outer membrane protein A (OmpA) from E. coli is a key component of bacterial outer membranes.
  • Understanding the oligomeric states and structures of OmpA is crucial for deciphering its function.

Purpose of the Study:

  • To analyze the collisional cross section (CCS) of oligomeric states of E. coli outer membrane OmpA.
  • To provide structural insights into OmpA oligomers using ion-mobility mass spectrometry.

Main Methods:

  • Gas-phase collisional cross section (CCS) measurements.
  • Ion-mobility mass spectrometry (IM-MS).

Main Results:

  • CCS was measured for different oligomeric states of E. coli OmpA.

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  • The CCS of the OmpA dimer supports a specific structural model.

    • Conclusions:

    • The structural model supported by the dimer's CCS involves paired periplasmic C-terminal domains.
    • These domains project away from the transmembrane porin structures.