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Siderophore-Binding Periplasmatic Protein FhuD and Related Periplasmic Binding Proteins Involved in Bacterial Iron Uptake

Part 1. Iron

Non-Heme Proteins: Iron Transport

  1. Karla D. Krewulak1,
  2. Wolfgang Köster2,
  3. Hans J. Vogel1

Published Online: 15 SEP 2009

DOI: 10.1002/0470028637.met251

Handbook of Metalloproteins

Handbook of Metalloproteins

How to Cite

Krewulak, K. D., Köster, W. and Vogel, H. J. 2009. Siderophore-Binding Periplasmatic Protein FhuD and Related Periplasmic Binding Proteins Involved in Bacterial Iron Uptake. Handbook of Metalloproteins. 1.

Author Information

  1. 1

    University of Calgary, Structural Biology Research Group, Department of Biological Sciences, Calgary, Alberta, Canada

  2. 2

    University of Saskatchewan, VIDO-Vaccine & Infectious Diseases Organization, Saskatoon, Saskatchewan, Canada

Publication History

  1. Published Online: 15 SEP 2009

Abstract

To fulfill their nutritional requirement for iron, many microorganisms synthesize low-molecular-weight iron-chelating compounds called siderophores. These iron sources are transported into the gram-negative bacterial cell via specific uptake pathways that include an outer membrane receptor, a periplasmic binding protein (PBP), and an inner membrane ATP-binding cassette (ABC) transporter. Gram-positive bacteria lack an outer membrane, and thus the uptake of the ferric siderophore involves a membrane-anchored PBP and an ABC transporter. Siderophores are classified as hydroxamate, catecholate, or hydroxycarboxylate type siderophores. This review details what is currently known about the PBP, FhuD (Fhu — ferric hydroxamate uptake), involved in the uptake of hydroxamate-type siderophores. In addition, several structurally related periplasmic binding proteins that mediate bacterial metal ion transport are also discussed.

3D Structure

Keywords:

  • bacterial iron uptake;
  • periplasmic binding protein;
  • iron;
  • heme;
  • siderophore;
  • transferrin;
  • FhuD;
  • BtuF;
  • TroA;
  • ZnuA;
  • ShuT