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Surface loop motion in FepA.

Daniel C Scott1, Salete M C Newton, Phillip E Klebba

  • 1Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA.

Journal of Bacteriology
|August 10, 2002
PubMed
Summary
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Conformational changes in Escherichia coli FepA loops were observed during ferric enterobactin transport. Ligand binding induces an approximate 15 Å shift, transitioning FepA from an open to a closed state.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Escherichia coli FepA is an outer membrane protein crucial for siderophore-mediated iron uptake.
  • Understanding FepA's conformational dynamics is key to elucidating its transport mechanism.

Purpose of the Study:

  • To investigate the conformational motion of surface loops in Escherichia coli FepA during ferric enterobactin transport.
  • To determine the structural changes associated with ligand binding and transport.

Main Methods:

  • Utilized a lysine-specific cleavable cross-linking reagent, ethylene glycolbis(sulfosuccimidylsuccinate) (Sulfo-EGS).
  • Employed site-directed mutagenesis to identify reactive lysine residues.
  • Analyzed cross-linking products to map protein-protein interactions and conformational states.

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Main Results:

  • Sulfo-EGS cross-linked specific lysine residues (K332 and K483) in FepA's surface loops.
  • Ferric enterobactin binding blocked cross-linking to other outer membrane proteins (OmpF, OmpC, OmpA) and reduced cross-linking to K332.
  • These findings indicate a ligand-induced conformational change of approximately 15 Å in FepA loops.

Conclusions:

  • Escherichia coli FepA undergoes significant conformational changes in its surface loops upon ferric enterobactin binding.
  • The transition is from an open, ligand-free state to a closed, ligand-bound state.
  • These conformational shifts are essential for the siderophore transport process.