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Structure of YraM, a protein essential for growth of Haemophilus influenzae

J Vijayalakshmi1, Brian J Akerley, Mark A Saper

  • 1Biophysics, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.

Proteins
|April 17, 2008
PubMed

Insights

Nontypeable Haemophilus influenzae YraM-C protein structure reveals a novel binding pocket. This finding could lead to new therapeutic strategies against this important human pathogen.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Nontypeable Haemophilus influenzae causes significant childhood infections and exacerbates COPD.
  • No vaccines are currently available for this pathogen.
  • The essential protein YraM's function remains unknown.

Purpose of the Study:

  • To determine the structure of the carboxyl-terminal module of YraM (YraM-C).
  • To elucidate the potential function of YraM in H. influenzae.

Main Methods:

  • Crystallization of YraM-C (residues 257-573).
  • Structure determination using multiwavelength anomalous diffraction (MAD).
  • Model refinement to 1.35 Å resolution.

Main Results:

  • The YraM-C structure reveals a fold similar to periplasmic binding proteins (PBPs).
  • Conserved residues suggest a ligand-binding site between the two domains.
  • Modeling indicates a putative binding pocket larger than typical PBP sites.

Conclusions:

  • YraM-C shares structural homology with PBPs, suggesting a role in ligand binding.
  • The unique binding pocket may indicate a novel function for YraM.
  • Further research into YraM's function could inform new therapeutic targets.

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