Siderophore-Binding Periplasmatic Protein FhuD and Related Periplasmic Binding Proteins Involved in Bacterial Iron Uptake
Part 1. Iron
Non-Heme Proteins: Iron Transport
Published Online: 15 SEP 2009
Copyright © 2006 John Wiley & Sons, Ltd. All rights reserved.
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.
- Published Online: 15 SEP 2009
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.
- bacterial iron uptake;
- periplasmic binding protein;