Close before opening

Science. 2002 Mar 1;295(5560):1658-9. doi: 10.1126/science.1070129.

Abstract

As bacteria need iron from the environment to survive, they have evolved active iron transporter proteins in their outer membranes. In her Perspective, Postle discusses new insights into iron transport revealed by the crystal structure of the iron transporter FecA in E. coli (Ferguson et al.).

Publication types

  • Comment

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / metabolism
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Biological Transport, Active
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • Crystallography, X-Ray
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism
  • Ferric Compounds / metabolism*
  • Ion Channel Gating
  • Ligands
  • Membrane Proteins / metabolism
  • Models, Biological
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Receptors, Cell Surface*
  • Siderophores / metabolism

Substances

  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • FecA protein, E coli
  • Ferric Compounds
  • Ligands
  • Membrane Proteins
  • Receptors, Cell Surface
  • Siderophores
  • tonB protein, Bacteria
  • tonB protein, E coli
  • ferric citrate