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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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Structure of the OmpA-like domain of RmpM from Neisseria meningitidis

Sylvestre Grizot1, Susan K Buchanan

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health , Department of Health and Human Services, Bethesda, Maryland 20892, USA.

Molecular Microbiology
|February 7, 2004
PubMed

Insights

The structure of RmpM, a Neisseria meningitidis protein, reveals a peptidoglycan binding site. This finding suggests RmpM may dimerize to enhance binding and stabilize outer membrane proteins.

Area of Science:

  • Microbiology
  • Structural Biology
  • Bacterial Outer Membrane Proteins

Background:

  • RmpM is a protein from Neisseria meningitidis known to interact with outer membrane proteins.
  • These interactions are crucial for bacterial cell structure and function.

Purpose of the Study:

  • To determine the crystal structure of the C-terminal domain of RmpM.
  • To identify potential peptidoglycan binding sites and understand RmpM's role in the bacterial cell envelope.

Main Methods:

  • X-ray crystallography to obtain the 1.9 Å crystal structure of the RmpM C-terminal domain.
  • Solution experiments to investigate RmpM's oligomeric state.

Main Results:

  • The C-terminal domain of RmpM adopts a betaalphabetaalphabetabeta fold, homologous to Escherichia coli OmpA's C-terminal domain.
  • A putative peptidoglycan binding site was identified, along with key residues potentially involved in binding.
  • Evidence suggests RmpM may exist as a dimer, potentially enhancing peptidoglycan binding efficiency.

Conclusions:

  • The RmpM C-terminal domain's structure provides insights into its peptidoglycan binding mechanism.
  • Dimerization of RmpM could facilitate simultaneous binding to multiple peptidoglycan chains.
  • RmpM may play a dual role in peptidoglycan binding and stabilizing outer membrane protein complexes.

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