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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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Low-resolution structures of OmpA⋅DDM protein-detergent complexes.

Jørn Døvling Kaspersen1, Christian Moestrup Jessen, Brian Stougaard Vad

  • 1Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, 8000 Aarhus C (Denmark); Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C (Denmark).

Chembiochem : a European Journal of Chemical Biology
|August 21, 2014
PubMed
Summary

We used SAXS to reveal the structure of E. coli OmpA protein in detergent. Monomers and linked dimers fold as expected, but other forms are complex.

Keywords:
membrane proteinsmicellesouter-membrane protein Aprotein/detergent stoichiometrysmall-angle X-ray scattering

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Proteins

Background:

  • Outer-membrane proteins (OMPs) are crucial for bacterial cell structure and function.
  • Understanding OMP structure in membrane-mimicking environments is essential for drug development.
  • Escherichia coli outer-membrane protein A (OmpA) is a well-studied model system.

Purpose of the Study:

  • To determine the low-resolution structure of OmpA variants using Small-Angle X-ray Scattering (SAXS).
  • To investigate the structural behavior of OmpA monomers, dimers, and full-length protein in a dodecyl maltoside (DDM) micelle environment.
  • To model the OmpA structures within an amphiphilic environment.

Main Methods:

  • Small-Angle X-ray Scattering (SAXS) was employed to analyze protein structures.
  • Three variants of the OmpA transmembrane domain (monomers, self-associated dimers, covalently linked dimers) were studied.
  • The monomeric species of full-length OmpA, including the periplasmic domain, was also analyzed.

Main Results:

  • Monomeric and covalently linked OmpA dimers were successfully modeled as one and two folded proteins in DDM micelles, respectively.
  • Noncovalently linked OmpA dimers exhibited a more complex structure, potentially involving higher-order associations.
  • The full-length OmpA structure consists of a globular periplasmic domain linked to the transmembrane domain via a flexible linker.

Conclusions:

  • SAXS provides valuable insights into the structure of OmpA in amphiphilic environments.
  • The study elucidates the structural organization of OmpA monomers and dimers within detergent micelles.
  • The findings contribute to understanding how membrane proteins embed and function within lipid bilayers.